5V00

Structure of HutD from Pseudomonas fluorescens SBW25 (Formate condition)

Replaces:  3ESG

Summary for 5V00

• Entry DOI: 10.2210/pdb5v00/pdb
• Related: 5FCC
• Descriptor: Uncharacterized protein, GLYCEROL, FORMIC ACID, ... (4 entities in total)
• Functional Keywords: bicupin, histidine degradation, unknown function
• Biological source: Pseudomonas fluorescens (strain SBW25)
• Total number of polymer chains: 2
• Total formula weight: 43142.40

Authors

Liu, Y.,Johnston, J.M.,Gerth, M.L.,Baker, E.N.,Lott, J.S.,Rainey, P.B. (deposition date: 2017-02-27, release date: 2017-03-15, Last modification date: 2023-10-04)

Primary citation

Gerth, M.L.,Liu, Y.,Jiao, W.,Zhang, X.X.,Baker, E.N.,Lott, J.S.,Rainey, P.B.,Johnston, J.M.
Crystal structure of a bicupin protein HutD involved in histidine utilization in Pseudomonas.
Proteins, 85:1580-1588, 2017

PubMed 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.

PubMed: 28383128
DOI: 10.1002/prot.25303

Experimental method

X-RAY DIFFRACTION (1.8 Å)