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

Authors :
Gerth ML
Liu Y
Jiao W
Zhang XX
Baker EN
Lott JS
Rainey PB
Johnston JM
Source :
Proteins [Proteins] 2017 Aug; Vol. 85 (8), pp. 1580-1588. Date of Electronic Publication: 2017 Apr 25.
Publication Year :
2017

Abstract

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 Å 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. © 2017 Wiley Periodicals, Inc.<br /> (© 2017 Wiley Periodicals, Inc.)

Details

Language :
English
ISSN :
1097-0134
Volume :
85
Issue :
8
Database :
MEDLINE
Journal :
Proteins
Publication Type :
Academic Journal
Accession number :
28383128
Full Text :
https://doi.org/10.1002/prot.25303