2h92
From Proteopedia
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Crystal Structure of Staphylococcus aureus Cytidine Monophosphate Kinase in complex with cytidine-5'-monophosphate
Overview
The crystal structure of Staphylococcus aureus cytidine monophosphate kinase (CMK) in complex with cytidine 5'-monophosphate (CMP) has been determined at 2.3 angstroms 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 approximately 16 degrees 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.
About this Structure
2H92 is a Single protein structure of sequence from Staphylococcus aureus with , and as ligands. Active as Cytidylate kinase, with EC number 2.7.4.14 Full crystallographic information is available from OCA.
Reference
Structure of Staphylococcus aureus cytidine monophosphate kinase in complex with cytidine 5'-monophosphate., Dhaliwal B, Ren J, Lockyer M, Charles I, Hawkins AR, Stammers DK, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Aug 1;62(Pt, 8):710-5. Epub 2006 Jul 24. PMID:16880539
Page seeded by OCA on Thu Feb 21 17:39:26 2008
