dc.contributor.author |
Gerth, ML |
en |
dc.contributor.author |
Liu, Y |
en |
dc.contributor.author |
Jiao, W |
en |
dc.contributor.author |
Zhang, X-X |
en |
dc.contributor.author |
Baker, Edward |
en |
dc.contributor.author |
Lott, Jeremy |
en |
dc.contributor.author |
Rainey, PB |
en |
dc.contributor.author |
Johnston, Jodie |
en |
dc.date.accessioned |
2018-10-10T23:28:04Z |
en |
dc.date.issued |
2017-08 |
en |
dc.identifier.issn |
0887-3585 |
en |
dc.identifier.uri |
http://hdl.handle.net/2292/40662 |
en |
dc.description.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. |
en |
dc.format.medium |
Print-Electronic |
en |
dc.language |
eng |
en |
dc.relation.ispartofseries |
Proteins |
en |
dc.rights |
Items in ResearchSpace are protected by copyright, with all rights reserved, unless otherwise indicated. Previously published items are made available in accordance with the copyright policy of the publisher. |
en |
dc.rights.uri |
https://researchspace.auckland.ac.nz/docs/uoa-docs/rights.htm |
en |
dc.subject |
Pseudomonas fluorescens |
en |
dc.subject |
Escherichia coli |
en |
dc.subject |
Glutamates |
en |
dc.subject |
Histidine |
en |
dc.subject |
Bacterial Proteins |
en |
dc.subject |
Recombinant Proteins |
en |
dc.subject |
Crystallography, X-Ray |
en |
dc.subject |
Cloning, Molecular |
en |
dc.subject |
Gene Expression |
en |
dc.subject |
Binding Sites |
en |
dc.subject |
Amino Acid Motifs |
en |
dc.subject |
Protein Binding |
en |
dc.subject |
Biological Transport |
en |
dc.subject |
Models, Molecular |
en |
dc.subject |
Protein Interaction Domains and Motifs |
en |
dc.subject |
Protein Conformation, alpha-Helical |
en |
dc.subject |
Protein Conformation, beta-Strand |
en |
dc.title |
Crystal structure of a bicupin protein HutD involved in histidine utilization in Pseudomonas. |
en |
dc.type |
Journal Article |
en |
dc.identifier.doi |
10.1002/prot.25303 |
en |
pubs.issue |
8 |
en |
pubs.begin-page |
1580 |
en |
pubs.volume |
85 |
en |
dc.rights.holder |
Copyright: The author |
en |
dc.identifier.pmid |
28383128 |
en |
pubs.end-page |
1588 |
en |
pubs.publication-status |
Published |
en |
dc.rights.accessrights |
http://purl.org/eprint/accessRights/RestrictedAccess |
en |
pubs.subtype |
Journal Article |
en |
pubs.elements-id |
622718 |
en |
pubs.org-id |
Science |
en |
pubs.org-id |
Biological Sciences |
en |
pubs.org-id |
Science Research |
en |
pubs.org-id |
Maurice Wilkins Centre (2010-2014) |
en |
dc.identifier.eissn |
1097-0134 |
en |
pubs.record-created-at-source-date |
2017-04-06 |
en |
pubs.dimensions-id |
28383128 |
en |