Crystal structure of a bicupin protein HutD involved in histidine utilization in Pseudomonas

被引：2

作者：

Gerth, M. L. ^{[1
,6
]}

Liu, Y. ^{[1
]}

Jiao, W. ^{[2
]}

Zhang, X. -X. ^{[1
]}

Baker, E. N. ^{[3
]}

Lott, J. S. ^{[3
]}

Rainey, P. B. ^{[1
,4
,5
]}

Johnston, J. M. ^{[3
]}

机构：

[1] Massey Univ Albany, New Zealand Inst Adv Study, Auckland, New Zealand

[2] Univ Canterbury, Biomol Interact Ctr, Christchurch, New Zealand

[3] Univ Auckland, Sch Biol Sci, Private Bag 92019, Auckland, New Zealand

[4] PSL Res Univ, Ecole Super Phys & Chim Ind Ville Paris, ESPCI ParisTech, CNRS UMR 8231, F-75231 Paris 05, France

[5] Max Planck Inst Evolutionary Biol, Dept Microbial Populat Biol, August Thiennemann Str 2, D-24306 Plon, Germany

[6] Univ Otago, Dept Biochem, POB 56, Dunedin 9054, New Zealand

来源：

PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS | 2017年 / 85卷 / 08期

关键词：

cupin; crystal structure; ligand binding; SUPERFAMILY; CONSERVATION; REFINEMENT;

D O I：

10.1002/prot.25303

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：

Cupins form one of the most functionally diverse superfamilies of proteins, with members performing a wide range of catalytic, non-catalytic, and regulatory functions. HutD is a predicted bicupin protein that is involved in histidine utilization (Hut) in Pseudomonas species. Previous genetic analyses have suggested that it limits the upper level of Hut pathway expression, but its mechanism of action is unknown. Here, we have determined the structure of PfluHutD at 1.74 angstrom resolution in several crystallization conditions, and identified N-formyl-l-glutamate (FG, a Hut pathway intermediate) as a potential ligand in vivo. Proteins 2017; 85:1580-1588. (c) 2017 Wiley Periodicals, Inc.

引用

页码：1580 / 1588

页数：9

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