6B0U

Crystal structure of acetyltransferase Eis from Mycobacterium tuberculosis in complex with a Lys-containing peptide

6B0U の概要

• エントリーDOI: 10.2210/pdb6b0u/pdb
• 分子名称: N-acetyltransferase Eis, Synthetic peptide ATKAPAKKA, COENZYME A (3 entities in total)
• 機能のキーワード: histone acetylation, aminoglycoside, drug resistance, tuberculosis, acetylation, transferase
• 由来する生物種: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv); 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 145692.54

構造登録者

Biswas, T.,Pang, A.H.,Garneau-Tsodikova, S.,Tsodikov, O.V. (登録日: 2017-09-15, 公開日: 2018-01-31, 最終更新日: 2024-11-06)

主引用文献

Green, K.D.,Biswas, T.,Pang, A.H.,Willby, M.J.,Reed, M.S.,Stuchlik, O.,Pohl, J.,Posey, J.E.,Tsodikov, O.V.,Garneau-Tsodikova, S.
Acetylation by Eis and Deacetylation by Rv1151c of Mycobacterium tuberculosis HupB: Biochemical and Structural Insight.
Biochemistry, 57:781-790, 2018

PubMed Abstract: Bacterial nucleoid-associated proteins (NAPs) are critical to genome integrity and chromosome maintenance. Post-translational modifications of bacterial NAPs appear to function similarly to their better studied mammalian counterparts. The histone-like NAP HupB from Mycobacterium tuberculosis (Mtb) was previously observed to be acetylated by the acetyltransferase Eis, leading to genome reorganization. We report biochemical and structural aspects of acetylation of HupB by Eis. We also found that the SirT-family NAD-dependent deacetylase Rv1151c from Mtb deacetylated HupB in vitro and characterized the deacetylation kinetics. We propose that activities of Eis and Rv1151c could regulate the acetylation status of HupB to remodel the mycobacterial chromosome in response to environmental changes.

PubMed: 29345920
DOI: 10.1021/acs.biochem.7b01089

実験手法

X-RAY DIFFRACTION (2.8 Å)