Universality of critical active site glutamate as an acid–base catalyst in serine hydroxymethyltransferase function

Drago, Victoria N.; Phillips, Robert S.; Kovalevsky, Andrey

doi:10.1039/D4SC03187C

Universality of critical active site glutamate as an acid–base catalyst in serine hydroxymethyltransferase function

Journal Article · Wed Aug 14 00:00:00 EDT 2024 · Chemical Science

DOI:https://doi.org/10.1039/D4SC03187C· OSTI ID:2403379

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Neutron Scattering Division, Oak Ridge National Laboratory, Oak Ridge, TN, 37831, USA
Department of Chemistry, University of Georgia, Athens, GA, 30602, USA, Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA, 30602, USA

Neutron crystallography revealed protonation states in Tth SHMT-FA complex. Glu53 is protonated but other residues maintain protonation states upon FA binding. Structural analyses support key roles of Glu53 and gating loop dynamics in SHMT function.

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Research Organization:: Argonne National Laboratory (ANL), Argonne, IL (United States). Advanced Photon Source (APS); Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States). Center for Structural Molecular Biology (CSMB); Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States). Spallation Neutron Source (SNS)

Sponsoring Organization:: National Institutes of Health (NIH); USDOE; USDOE Office of Science (SC), Basic Energy Sciences (BES); USDOE Office of Science (SC), Biological and Environmental Research (BER)

Grant/Contract Number:: AC02-06CH11357; AC05-00OR22725

OSTI ID:: 2403379

Alternate ID(s):: OSTI ID: 2434365

Journal Information:: Chemical Science, Journal Name: Chemical Science Journal Issue: 32 Vol. 15; ISSN 2041-6520; ISSN CSHCBM

Publisher:: Royal Society of Chemistry (RSC)Copyright Statement

Country of Publication:: United Kingdom

Language:: English

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