Crystal structure of a member of a novel family of dioxygenases (PF10014) reveals a conserved cupin fold and active site

被引：10

作者：

Xu, Qingping ^{[1
,2
]}

Grant, Joanna ^{[1
,3
]}

Chiu, Hsiu-Ju ^{[1
,2
]}

Farr, Carol L. ^{[1
,4
]}

Jaroszewski, Lukasz ^{[1
,5
,6
]}

Knuth, Mark W. ^{[1
,3
]}

Miller, Mitchell D. ^{[1
,2
]}

Lesley, Scott A. ^{[1
,3
,4
]}

Godzik, Adam ^{[1
,5
,6
]}

Elsliger, Marc-Andre ^{[1
,4
]}

Deacon, Ashley M. ^{[1
,2
]}

Wilson, Ian A. ^{[1
,4
]}

机构：

[1] Joint Ctr Struct Genom, La Jolla, CA USA

[2] SLAC Natl Accelerator Lab, Stanford Synchrotron Radiat Lightsource, Menlo Pk, CA 94025 USA

[3] Novartis Res Fdn, Genom Inst, Prot Sci Dept, San Diego, CA 92121 USA

[4] Scripps Res Inst, Dept Integrat Struct & Computat Biol, La Jolla, CA 92037 USA

[5] Univ Calif San Diego, Ctr Res Biol Syst, La Jolla, CA 92093 USA

[6] Sanford Burnham Med Res Inst, Program Bioinformat & Syst Biol, La Jolla, CA 92037 USA

来源：

PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS | 2014年 / 82卷 / 01期

关键词：

PF10014; BsmA; cupin dioxygenase; free amino acids; 2-oxyglutarate; ferrous iron; BIOSYNTHETIC GENE-CLUSTER; SERVER;

D O I：

10.1002/prot.24362

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：

PF10014 is a novel family of 2-oxyglutarate-Fe2+-dependent dioxygenases that are involved in biosynthesis of antibiotics and regulation of biofilm formation, likely by catalyzing hydroxylation of free amino acids or other related ligands. The crystal structure of a PF10014 member from Methylibium petroleiphilum at 1.9 angstrom resolution shows strong structural similarity to cupin dioxygenases in overall fold and active site, despite very remote homology. However, one of the -strands of the cupin catalytic core is replaced by a loop that displays conformational isomerism that likely regulates the active site. Proteins 2014; 82:164-170. (c) 2013 Wiley Periodicals, Inc.

引用

页码：164 / 170

页数：7

共 26 条

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