dc.contributor.author |
Johnston, Jodie |
en |
dc.contributor.author |
Jiang, M |
en |
dc.contributor.author |
Guo, ZH |
en |
dc.contributor.author |
Baker, Edward |
en |
dc.date.accessioned |
2011-12-06T02:32:18Z |
en |
dc.date.issued |
2010-08 |
en |
dc.identifier.citation |
Acta Crystallographica Section D Biological Crystallography 66(Pt 8):909-917 Aug 2010 |
en |
dc.identifier.issn |
0907-4449 |
en |
dc.identifier.uri |
http://hdl.handle.net/2292/9805 |
en |
dc.description.abstract |
Mycobacterium tuberculosis, the cause of tuberculosis, is a devastating human pathogen against which new drugs are urgently needed. Enzymes from the biosynthetic pathway for menaquinone are considered to be valid drug targets. The protein encoded by the open reading frame Rv0554 has been expressed, purified and subjected to structural and functional analysis to test for a putative role in menaquinone biosynthesis. The crystal structure of Rv0554 has been solved and refined in two different space groups at 2.35 and 1.9 Å resolution. The protein is dimeric, with an /-hydrolase monomer fold. In each monomer, a large cavity adjacent to the catalytic triad is enclosed by a helical lid. Dimerization is mediated by the lid regions. Small-molecule additives used in crystallization bind in the active site, but no binding of ligands related to menaquinone biosynthesis could be detected and functional assays failed to support possible roles in menaquinone biosynthesis. |
en |
dc.language |
EN |
en |
dc.publisher |
International Union of Crystallography |
en |
dc.relation.ispartofseries |
Acta Crystallographica Section D: Biological Crystallography |
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. Details obtained from
http://www.sherpa.ac.uk/romeo/issn/0907-4449/ |
en |
dc.rights.uri |
https://researchspace.auckland.ac.nz/docs/uoa-docs/rights.htm |
en |
dc.subject |
ALPHA/BETA-HYDROLASE FOLD |
en |
dc.subject |
MOLECULAR REPLACEMENT |
en |
dc.subject |
PROTEIN-PRODUCTION |
en |
dc.subject |
CRYSTAL-STRUCTURES |
en |
dc.subject |
ESCHERICHIA-COLI |
en |
dc.subject |
DRUG TARGETS |
en |
dc.subject |
IDENTIFICATION |
en |
dc.subject |
SYSTEM |
en |
dc.subject |
GROWTH |
en |
dc.subject |
VITAMIN-K-2 |
en |
dc.title |
Structural and functional analysis of Rv0554 from Mycobacterium tuberculosis: testing a putative role in menaquinone biosynthesis |
en |
dc.type |
Journal Article |
en |
dc.identifier.doi |
10.1107/S0907444910025771 |
en |
pubs.issue |
8 |
en |
pubs.begin-page |
909 |
en |
pubs.volume |
66 |
en |
dc.rights.holder |
Copyright: International Union of Crystallography |
en |
dc.identifier.pmid |
20693690 |
en |
pubs.end-page |
917 |
en |
dc.rights.accessrights |
http://purl.org/eprint/accessRights/OpenAccess |
en |
pubs.subtype |
Article |
en |
pubs.elements-id |
119924 |
en |
pubs.org-id |
Science |
en |
pubs.org-id |
Science Research |
en |
pubs.org-id |
Maurice Wilkins Centre (2010-2014) |
en |
pubs.record-created-at-source-date |
2011-12-06 |
en |
pubs.dimensions-id |
20693690 |
en |