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Lookup NU author(s): Professor Alastair Hawkins
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The crystal structure of Staphylococcus aureus cytidine monophosphate kinase (CMK) in complex with cytidine 5′-monophosphate (CMP) has been determined at 2.3 Å resolution. The active site reveals novel features when compared with two orthologues of known structure. Compared with the Streptococcus pneumoniae CMK solution structure of the enzyme alone, S. aureus CMK adopts a more closed conformation, with the NMP-binding domain rotating by ∼16° towards the central pocket of the molecule, thereby assembling the active site. Comparing Escherichia coli and S. aureus CMK-CMP complex structures reveals differences within the active site, including a previously unreported indirect interaction of CMP with Asp33, the replacement of a serine residue involved in the binding of CDP by Ala12 in S. aureus CMK and an additional sulfate ion in the E. coli CMK active site. The detailed understanding of the stereochemistry of CMP binding to CMK will assist in the design of novel inhibitors of the enzyme. Inhibitors are required to treat the widespread hospital infection methicillin-resistant S. aureus (MRSA), currently a major public health concern. © 2006 International Union of Crystallography All rights reserved.
Author(s): Dhaliwal B, Ren J, Lockyer M, Charles I, Hawkins AR, Stammers DK
Publication type: Article
Publication status: Published
Journal: Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Year: 2006
Volume: 62
Issue: 8
Pages: 710-715
ISSN (print): 1744-3091
ISSN (electronic):
Publisher: Wiley-Blackwell
URL: http://dx.doi.org/10.1107/S174430910602447X
DOI: 10.1107/S174430910602447X
PubMed id: 16880539
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