Crystal structure of Bacillus subtilis YabJ, a purine regulatory protein and member of the highly conserved YjgF family

被引：76

作者：

Sinha, S

Rappu, P

Lange, SC

Mäntsälä, P

Zalkin, H

Smith, JL ^{[1
]}

机构：

[1] Purdue Univ, Dept Biol Sci, W Lafayette, IN 47907 USA

[2] Purdue Univ, Dept Biochem, W Lafayette, IN 47907 USA

[3] Turku Univ, Dept Biochem & Food Chem, FIN-20014 Turku, Finland

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1999年 / 96卷 / 23期

关键词：

D O I：

10.1073/pnas.96.23.13074

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The yabJ gene in Bacillus subtilis is required for adenine-mediated repression of purine biosynthetic genes in vivo and codes for an acid-soluble, 14-kDa protein, The molecular mechanism of YabJ is unknown. YabJ is a member of a large, widely distributed family of proteins of unknown biochemical function. The 1.7-Angstrom crystal structure of YabJ reveals a trimeric organization with extensive buried hydrophobic surface and an internal water-filled cavity, The most important finding in the structure is a deep, narrow cleft between subunits lined with nine side chains that are invariant among the 25 most similar homologs. This conserved site is proposed to be a binding or catalytic site for a ligand or substrate that is common to YabJ and other members of the YER057c/YjgF/UK114 family of proteins.

引用

页码：13074 / 13079

页数：6

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