Three-dimensional structure of YaaE from Bacillus subtilis, a glutaminase implicated in pyridoxal-5′-phosphate biosynthesis

被引：37

作者：

Bauer, JA ^{[1
]}

Bennett, EM ^{[1
]}

Begley, TP ^{[1
]}

Ealick, SE ^{[1
]}

机构：

[1] Cornell Univ, Dept Chem & Biol Chem, Ithaca, NY 14853 USA

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 2004年 / 279卷 / 04期

关键词：

D O I：

10.1074/jbc.M310311200

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The structure of YaaE from Bacillus subtilis was determined at 2.5-Angstrom resolution. YaaE is a member of the triad glutamine aminotransferase family and functions in a recently identified alternate pathway for the biosynthesis of vitamin B-6. Proposed active residues include conserved Cys-79, His-170, and Glu-172. YaaE shows similarity to HisH, a glutaminase involved in histidine biosynthesis. YaaD associates with YaaE. A homology model of this protein was constructed. YaaD is predicted to be a (beta/alpha)(8) barrel on the basis of sequence comparisons. The predicted active site includes highly conserved residues 211-216 and 233-235. Finally, a homology model of a putative YaaD-YaaE complex was prepared using the structure of HisH-F as a model. This model predicts that the ammonia molecule generated by YaaE is channeled through the center of the YaaD barrel to the putative YaaD active site.

引用

页码：2704 / 2711

页数：8

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