6IOI

Crystal structure of Homoserine O-acetyltransferase in complex with CoA from Mycobacterium smegmatis ATCC 19420

6IOI の概要

• エントリーDOI: 10.2210/pdb6ioi/pdb
• 分子名称: Homoserine O-acetyltransferase, COENZYME A (3 entities in total)
• 機能のキーワード: transferase, biosynthetic protein
• 由来する生物種: Mycobacterium smegmatis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 80487.05

構造登録者

Sagong, H.-Y.,Kim, K.-J. (登録日: 2018-10-30, 公開日: 2019-09-04, 最終更新日: 2023-11-22)

主引用文献

Sagong, H.Y.,Hong, J.,Kim, K.J.
Crystal structure and biochemical characterization of O-acetylhomoserine acetyltransferase from Mycobacterium smegmatis ATCC 19420.
Biochem.Biophys.Res.Commun., 517:399-406, 2019

PubMed Abstract: Mycobacterium smegmatis is a good model for studying the physiology and pathogenesis of Mycobacterium tuberculosis due to its genetic similarity. As methionine biosynthesis exists only in microorganisms, the enzymes involved in methionine biosynthesis can be a potential target for novel antibiotics. Homoserine O-acetyltransferase from M. smegmatis (MsHAT) catalyzes the transfer of acetyl-group from acetyl-CoA to homoserine. To investigate the molecular mechanism of MsHAT, we determined its crystal structure in apo-form and in complex with either CoA or homoserine and revealed the substrate binding mode of MsHAT. A structural comparison of MsHAT with other HATs suggests that the conformation of the α5 to α6 region might influence the shape of the dimer. In addition, the active site entrance shows an open or closed conformation and might determine the substrate binding affinity of HATs.

PubMed: 31378370
DOI: 10.1016/j.bbrc.2019.07.117

実験手法

X-RAY DIFFRACTION (1.6 Å)