Anuj Kumar (@AnujR2d2) profile picture

Anuj Kumar

@AnujR2d2

CryoEM, Structural biology, Bioenergetics

 Marburg
Joined August 2020
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  • Followers97
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Photo by Anuj Kumar (@AnujR2d2)Photo by Anuj Kumar (@AnujR2d2)Photo by Anuj Kumar (@AnujR2d2)Photo by Anuj Kumar (@AnujR2d2)Photo by Anuj Kumar (@AnujR2d2)Photo by Anuj Kumar (@AnujR2d2)Photo by Anuj Kumar (@AnujR2d2)
For decades, how methanogenic archaea activate the MCR complex to produce methane remained a mystery. Today in Nature, we report the high-resolution cryo-EM structure of the MCR activation complex! 🥳🥳 nature.com/articles/s41586-0…
Structure of the ATP-driven methyl-coenzyme M reductase activation complex

Structure of the ATP-driven methyl-coenzyme M reductase activation complex

Nature - The structure and function of the MCR activation complex from Methanococcus maripaludis were revealed, demonstrating its ATP-dependent ability to activate MCR and form methane while...

nature.com
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We untangled the weird evolution of an NRPS. For the NRPS people. Check out the supps and you can see in detail how NRPS extend and shrink. I think its very beautiful. For the evolution people: Endless peptides form most beautiful.
Georg Hochberg (@KaHochberg) profile pictureGeorg Hochberg@KaHochbergOct 21
Haven't used this is in a while, but a new paper from the group is a good excuse. This is monster of a paper from Sebastian Kaiser about the evolution of non-ribosomal peptides. nature.com/articles/s41559-0…
Drift, selection and recombination bias drive the evolution of a non-ribosomal peptide

Drift, selection and recombination bias drive the evolution of a non-ribosomal peptide

Nature Ecology & Evolution - The structural diversity of non-ribosomal peptides is largely determined by recombination. This study shows that selection, genetic drift and biased recombination...

nature.com
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Our latest work on the nitrogenase-like methylthio-alkane reductase is now out @NatureCatalysis doi.org/10.1038/s41929-025-0… We biochemically and structurally characterized the methylthio-alkane reductase, a metalloenzyme that can produce ethylene from organic sulfur compounds.
Methylthio-alkane reductases use nitrogenase metalloclusters for carbon–sulfur bond cleavage

Methylthio-alkane reductases use nitrogenase metalloclusters for carbon–sulfur bond cleavage

Nature Catalysis - Methylthio-alkane reductases are recently discovered enzymes that can produce methanethiol and small hydrocarbons from methylated sulfur compounds. Now the cryo-EM structure of a...

nature.com
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It is out now 🥳🥂 I am very happy to be part of this nice collaboration in which we were able to characterize different bacterial chemoreceptors and their ligand specificities. Amazing teamwork with Wenhao Xu, @sourjik, @BangeBalcony, et. al 🤩 👇👇👇 pnas.org/doi/10.1073/pnas.25…
Specificities of chemosensory receptors in the human gut microbiota | PNAS

Specificities of chemosensory receptors in the human gut microbiota | PNAS

The human gut is rich in metabolites and harbors a complex microbial community, yet surprisingly little is known about the spectrum of chemical sig...

pnas.org
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I am honored and excited that our research on #nitrogenases and the conversion of #CO2 to hydrocarbons is highlighted in the Yearbook 2024 of the Max Planck Society, see page 29. An English and a German version of the Yearbook are available mpg.de/13631298/yearbook-hig….
Yearbook Highlights

Yearbook Highlights

The Yearbook Highlights of the Max Planck Society

mpg.de
Max Planck Society (@maxplanckpress) profile pictureMax Planck Society@maxplanckpress26 Jun 2025
Can't enough of science? Worry not - we've got you covered! 😊Our 2024 Yearbook Highlights Research just dropped: filled with inspiring science that shapes our future, from breakthroughs in heart health to ingenious ways to cut waste. Read all here➡️mpg.de/jahrbuch-highlights
Abstrakte Grafik mit Blättern und geometrischen Formen, ergänzt durch den Text „Sovereignty, Highlights 2024“ aus dem Jahrbuch der Max-Planck-Gesellschaft. Credit: MPG/mattweis

ALT Abstrakte Grafik mit Blättern und geometrischen Formen, ergänzt durch den Text „Sovereignty, Highlights 2024“ aus dem Jahrbuch der Max-Planck-Gesellschaft. Credit: MPG/mattweis

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New paper from the lab from @SriramGarg. We introduce a general substitution matrix for structural phylogenetics. I think this is a big deal, so read on below if you think deep history is important. academic.oup.com/mbe/advance…
A General Substitution Matrix for Structural Phylogenetics

A General Substitution Matrix for Structural Phylogenetics

Abstract. Sequence-based maximum likelihood phylogenetics is a widely used method for inferring evolutionary relationships, which has illuminated the evolu

academic.oup.com
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How do cells "decide" their fate from growth factor signals? Our new study introduces signaling homeorhesis — a dynamic alternative to homeostasis — to explain how cells interpret pulsatile signals into phenotypes. #CellBiology #CellSignaling
bioRxiv Cell Biology (@biorxiv_cellbio) profile picturebioRxiv Cell Biology@biorxiv_cellbio6 Jun 2025
Homeorhetic regulation of cellular phenotype biorxiv.org/content/10.1101/… #biorxiv_cellbio
Homeorhetic regulation of cellular phenotype

Homeorhetic regulation of cellular phenotype

How cells translate growth factor (GF) signals into context-specific phenotypes remains a fundamental question in cell biology. The classical view holds that cells translate a constant concentration...

biorxiv.org
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Anuj Kumar retweeted
nature (@Nature) profile picture
nature
@Nature19 Apr 2025
Nature research paper: Structure of the ATP-driven methyl-coenzyme M reductase activation complex go.nature.com/3Esgnmi
Structure of the ATP-driven methyl-coenzyme M reductase activation complex

Structure of the ATP-driven methyl-coenzyme M reductase activation complex

Nature - The structure and function of the MCR activation complex from Methanococcus maripaludis were revealed, demonstrating its ATP-dependent ability to activate MCR and form methane while...

nature.com
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I'm truly excited to announce our new publication in @Nature unraveling a central picture of the Methyl-coenzyme M reductase (MCR) activation machinery and it's strong ATP dependency - kudos to @AnujR2d2 for the fantastic illustration! LINK: nature.com/articles/s41586-0…
Image from Fidel Ramírez (@fidelormz)
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This is a wild paper. The anaerobic biochemistry is definitely worth your while (and beyond me to explain), but let me try to explain why this is also an evolutionary bombshell. This is about how nitrogen fixation evolved as we know it.
Fidel Ramírez (@fidelormz) profile pictureFidel Ramírez@fidelormz16 Apr 2025
I'm truly excited to announce our new publication in @Nature unraveling a central picture of the Methyl-coenzyme M reductase (MCR) activation machinery and it's strong ATP dependency - kudos to @AnujR2d2 for the fantastic illustration! LINK: nature.com/articles/s41586-0…
Image from Fidel Ramírez (@fidelormz)
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Check out this fantastic thread from @fidelormz about out latest work out in Nature!! 🥳🥳
Fidel Ramírez (@fidelormz) profile pictureFidel Ramírez@fidelormz16 Apr 2025
I'm truly excited to announce our new publication in @Nature unraveling a central picture of the Methyl-coenzyme M reductase (MCR) activation machinery and it's strong ATP dependency - kudos to @AnujR2d2 for the fantastic illustration! LINK: nature.com/articles/s41586-0…
Image from Fidel Ramírez (@fidelormz)
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This was a great effort and collaboration between me and my fellow co–first authors, @fidelormz and @sophia_pa_ 🥳🥳🥳 A blender image nicely illustrates our work :)
Image from Anuj Kumar (@AnujR2d2)
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I thank @SchullerJm for leading the team and conceptualising the project, and special thanks to @stripplab.bsky.social, Silvan, and @KaHochberg Also many thanks to Stefan for giving us generous access to kriosG4!!
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Take a moment to check the most recent publication by @AnujR2d2 et al., about the structure & mechanism of a major respiratory complex in anaerobes 👇🏼
Anuj Kumar (@AnujR2d2) profile pictureAnuj Kumar@AnujR2d28 Mar 2025
Excited to share our latest work on the structure and mechanism of the ancient sodium-pumping Rnf complex, now out in @NatureComms nature.com/articles/s41467-0…
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Excited to share our latest work on the structure and mechanism of the ancient sodium-pumping Rnf complex, now out in @NatureComms nature.com/articles/s41467-0…
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Very proud to share our latest work on the ancient the Na+-pumping Rnf complex – now out in Nature Comms. Thank you Schuller & Müller Labs for great collaboration, and @KAWstiftelsen for generous funding nature.com/articles/s41467-0…
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Two exciting papers about the the protection of nitrogenases from O2 by the ferredoxin Shethna protein II from the Tezcan doi.org/10.1038/s41586-024-0… and Einsle doi.org/10.1038/s41586-024-0… labs were published today by @Nature. Surprisingly both papers reveal superstructures of filaments.
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Great work from my colleague @TomasPascoa
Tomas Pascoa (@TomasPascoa) profile pictureTomas Pascoa@TomasPascoa11 Nov 2024
Replying to @TomasPascoa
Great to see our manuscript detailing the ping-pong mechanism of human Ceramide Synthase 6 out now in @NatureSMB! An excellent collaboration between @DavidBSauer's lab @CmdOxford, Liz Carpenter, @Boehringer and @UZH_en link: doi.org/10.1038/s41594-024-0… PDF: rdcu.be/dZOJP
Structural basis of the mechanism and inhibition of a human ceramide synthase

Structural basis of the mechanism and inhibition of a human ceramide synthase

Nature Structural & Molecular Biology - Pascoa et al. reveal structures of the human ceramide synthase 6 and elucidate the enzyme’s mechanism. Furthermore, the work uncovers the basis of...

nature.com
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Our latest work on a #nitrogenase-like enzyme, the methylthio-alkane reductase which surprisingly also contains large nitrogenase metalloclusters, the P-cluster and the [Fe8S9C]- (L)-cluster is now online: doi.org/10.1101/2024.10.19.6… Have a look at the 🧵 by @AnaLagoMaciel.
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I will be hiring officially later this year, but if you are interested in pursuing a Phd focused on metalloenzymes and infrared spectroscopy... Give me call!
Image from Sven T. Stripp 🇺🇦🔥🌊 (@stripp_lab)
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