Author

U. Ermler

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 3 Biophysics· 1

Signature Assays, Organisms & Methods

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Organism:bacteria (other)· 2 Assay:cryo-EM· 2 Approach:experimental assay· 2 Research Focus:protein structure prediction· 2 Research Focus:chromatin & epigenetic regulation· 1 Approach:deep learning· 1 Organism:E. coli· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

M. Gehl· 2 shared S. Shima· 2 shared S. Welsch· 2 shared U. Demmer· 2 shared A. Katsyv· 1 shared A. R. Mehdipour· 1 shared C. Himmrichs· 1 shared C. Muenke· 1 shared

Activity by Year

2021-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 16 mutual co-author links

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2 shared papersBiochemistry

M. Gehl

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Convergent evolution of (beta alpha)8-barrel fold methylene-tetrahydropterin reductases utilizing a common catalytic mechanism

M. Gehl, U. Demmer, U. Ermler, S. Shima

This paper identifies a common catalytic mechanism among methylene-tetrahydropterin reductases despite low sequence identity and convergent evolution.

bioRxiv · Sep 18, 2023 · PreprintBiochemistry

Crystal structure of FAD-independent methylene-tetrahydrofolate reductase from Mycobacterium hassiacum

M. Gehl, U. Demmer, U. Ermler, S. Shima

The paper reports the crystal structure of Mfr from M. hassiacum, showing structural similarity to MTHFR despite different catalytic mechanisms and coenzyme specificity.

bioRxiv · Nov 18, 2022Biochemistry

Structure-based electron-confurcation mechanism of the Ldh-EtfAB complex

U. Ermler, K. Kayastha, A. Katsyv, C. Himmrichs, S. Welsch, J. M. Schuller, V. Müller

The paper elucidates the structure-based electron-confurcation mechanism of the Ldh-EtfAB complex in Acetobacterium woodii using cryo-EM and AlphaFold2, revealing key redox states and interactions.

bioRxiv · Feb 2, 2022Biochemistry

Cryo-EM structures of pentameric autoinducer-2 exporter from E. coli reveal its transport mechanism

R. Khera, A. R. Mehdipour, J. R. Bolla, J. Kahnt, S. Welsch, U. Ermler, C. Muenke, C. V. Robinson, G. Hummer, H. Xie, H. Michel

The paper reports cryo-EM structures of AI-2 exporters from E. coli, revealing their pentameric structure and elevator-type transport mechanism.

bioRxiv · Oct 20, 2021 · PreprintBiophysics