4MVA

1.43 Angstrom Resolution Crystal Structure of Triosephosphate Isomerase (tpiA) from Escherichia coli in Complex with Acetyl Phosphate.

4MVA の概要

• エントリーDOI: 10.2210/pdb4mva/pdb
• 関連するPDBエントリー: 4K6A
• 分子名称: Triosephosphate isomerase, CHLORIDE ION, ACETYLPHOSPHATE, ... (7 entities in total)
• 機能のキーワード: structural genomics, niaid, national institute of allergy and infectious diseases, center for structural genomics of infectious diseases, csgid, tim beta/alpha barrel, triose-phosphate isomerase activity, isomerase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 60136.20

構造登録者

Minasov, G.,Kuhn, M.L.,Dubrovska, I.,Winsor, J.,Shuvalova, L.,Grimshaw, S.,Kwon, K.,Anderson, W.F.,Center for Structural Genomics of Infectious Diseases (CSGID) (登録日: 2013-09-23, 公開日: 2014-04-16, 最終更新日: 2023-09-20)

主引用文献

Kuhn, M.L.,Zemaitaitis, B.,Hu, L.I.,Sahu, A.,Sorensen, D.,Minasov, G.,Lima, B.P.,Scholle, M.,Mrksich, M.,Anderson, W.F.,Gibson, B.W.,Schilling, B.,Wolfe, A.J.
Structural, kinetic and proteomic characterization of acetyl phosphate-dependent bacterial protein acetylation.
Plos One, 9:e94816-e94816, 2014

PubMed Abstract: The emerging view of Nε-lysine acetylation in eukaryotes is of a relatively abundant post-translational modification (PTM) that has a major impact on the function, structure, stability and/or location of thousands of proteins involved in diverse cellular processes. This PTM is typically considered to arise by the donation of the acetyl group from acetyl-coenzyme A (acCoA) to the ε-amino group of a lysine residue that is reversibly catalyzed by lysine acetyltransferases and deacetylases. Here, we provide genetic, mass spectrometric, biochemical and structural evidence that Nε-lysine acetylation is an equally abundant and important PTM in bacteria. Applying a recently developed, label-free and global mass spectrometric approach to an isogenic set of mutants, we detected acetylation of thousands of lysine residues on hundreds of Escherichia coli proteins that participate in diverse and often essential cellular processes, including translation, transcription and central metabolism. Many of these acetylations were regulated in an acetyl phosphate (acP)-dependent manner, providing compelling evidence for a recently reported mechanism of bacterial Nε-lysine acetylation. These mass spectrometric data, coupled with observations made by crystallography, biochemistry, and additional mass spectrometry showed that this acP-dependent acetylation is both non-enzymatic and specific, with specificity determined by the accessibility, reactivity and three-dimensional microenvironment of the target lysine. Crystallographic evidence shows acP can bind to proteins in active sites and cofactor binding sites, but also potentially anywhere molecules with a phosphate moiety could bind. Finally, we provide evidence that acP-dependent acetylation can impact the function of critical enzymes, including glyceraldehyde-3-phosphate dehydrogenase, triosephosphate isomerase, and RNA polymerase.

PubMed: 24756028
DOI: 10.1371/journal.pone.0094816

実験手法

X-RAY DIFFRACTION (1.43 Å)