Structure of Escherichia coli UDP-N-acetylmuramoyl:L-alanine ligase (MurC)

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dc.contributor.author Deva, Taru en
dc.contributor.author Baker, Edward en
dc.contributor.author Squire, Christopher en
dc.contributor.author Smith, Clyde en
dc.date.accessioned 2016-08-11T04:15:15Z en
dc.date.issued 2006-12 en
dc.identifier.citation Acta Crystallographica Section D-Biological Crystallography, 2006, 62 pp. 1466 - 1474 (9) en
dc.identifier.issn 0907-4449 en
dc.identifier.uri http://hdl.handle.net/2292/29922 en
dc.description.abstract The bacterial cell wall provides essential protection from the external environment and confers strength and rigidity to counteract internal osmotic pressure. Without this layer the cell would be easily ruptured and it is for this reason that biosynthetic pathways leading to the formation of peptidoglycan have for many years been a prime target for effective antibiotics. Central to this pathway are four similar ligase enzymes which add peptide groups to glycan moieties. As part of a program to better understand the structure-function relationships in these four enzymes, the crystal structure of Escherichia coli UDP-N-acetylmuramoyl:L-alanine ligase (MurC) has been determined to 2.6 Å resolution. The structure was solved by multiwavelength anomalous diffraction methods from a single selenomethionine-substituted crystal and refined to a crystallographic R factor of 0.212 (Rfree = 0.259). The enzyme has a modular multi-domain structure very similar to those of other members of the mur family of ATP-dependent amide-bond ligases. Detailed comparison of these four enzymes shows that considerable conformational changes are possible. These changes, together with the recruitment of two different N-terminal domains, allow this family of enzymes to bind a substrate which is identical at one end and at the other has the growing peptide tail which will ultimately become part of the rigid bacterial cell wall. Comparison of the E. coli and Haemophilus influenzae structures and analysis of the sequences of known MurC enzymes indicate the presence of a `dimerization' motif in almost 50% of the MurC enzymes and points to a highly conserved loop in domain 3 that may play a key role in amino-acid ligand specificity. 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. en
dc.rights.uri https://researchspace.auckland.ac.nz/docs/uoa-docs/rights.htm en
dc.title Structure of Escherichia coli UDP-N-acetylmuramoyl:L-alanine ligase (MurC) en
dc.type Journal Article en
dc.identifier.doi 10.1107/S0907444906038376 en
pubs.issue 12 en
pubs.begin-page 1466 en
pubs.volume 62 en
dc.identifier.pmid 17139082 en
pubs.end-page 1474 en
dc.rights.accessrights http://purl.org/eprint/accessRights/RestrictedAccess en
pubs.subtype Article en
pubs.elements-id 71040 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
pubs.record-created-at-source-date 2010-09-01 en
pubs.dimensions-id 17139082 en


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