Crystal structure of a bicupin protein HutD involved in histidine utilization in Pseudomonas.
Proteins
; 85(8): 1580-1588, 2017 Aug.
Article
in En
| MEDLINE
| ID: mdl-28383128
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; 851580-1588. © 2017 Wiley Periodicals, Inc.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Bacterial Proteins
/
Pseudomonas fluorescens
/
Glutamates
/
Histidine
Type of study:
Prognostic_studies
Language:
En
Journal:
Proteins
Journal subject:
BIOQUIMICA
Year:
2017
Type:
Article
Affiliation country:
New Zealand