弗氏柠檬酸杆菌L-甲硫氨酸γ-裂解酶的结构
Structure of Citrobacter freundii L-methionine gamma-lyase.
作者信息
Mamaeva D V, Morozova E A, Nikulin A D, Revtovich S V, Nikonov S V, Garber M B, Demidkina T V
机构信息
Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov str. 32, 119991 Moscow, Russia.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Jun 1;61(Pt 6):546-9. doi: 10.1107/S1744309105015447.
Abstract
L-Methionine gamma-lyase (MGL) is a pyridoxal 5'-phosphate (PLP) dependent enzyme that catalyzes gamma-elimination of L-methionine. The crystal structure of MGL from Citrobacter freundii has been determined at 1.9 A resolution. The spatial fold of the protein is similar to those of MGLs from Pseudomonas putida and Trichomonas vaginalis. The comparison of these structures revealed that there are differences in PLP-binding residues and positioning of the surrounding flexible loops.
摘要
L-甲硫氨酸γ-裂合酶（MGL）是一种依赖于磷酸吡哆醛（PLP）的酶，可催化L-甲硫氨酸的γ-消除反应。弗氏柠檬酸杆菌MGL的晶体结构已在1.9埃分辨率下测定。该蛋白质的空间折叠与恶臭假单胞菌和阴道毛滴虫的MGL相似。这些结构的比较表明，PLP结合残基和周围柔性环的定位存在差异。
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