1w2g
CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS THYMIDYLATE KINASE COMPLEXED WITH DEOXYTHYMIDINE (DT) (2.1 A RESOLUTION)
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OverviewOverview
Tuberculosis (TB) is the primary cause of mortality among infectious, diseases. Mycobacterium tuberculosis thymidylate kinase (TMPK(Mtub)), catalyzes the ATP-dependent phosphorylation of deoxythymidine, 5'-monophosphate (dTMP). Essential to DNA replication, this enzyme, represents a promising target for developing new drugs against TB, because, the configuration of its active site is unique within the TMPK family., Indeed, it has been proposed that, as opposed to other TMPKs, catalysis by, TMPK(Mtub) necessitates the transient binding of a magnesium ion, coordinating the phosphate acceptor. Moreover, 3'-azidodeoxythymidine, monophosphate (AZTMP) is a competitive inhibitor of TMPK(Mtub), whereas it, is a substrate for human and other TMPKs. Here, the crystal structures of, TMPK(Mtub) in ... [(full description)]
About this StructureAbout this Structure
1W2G is a [Single protein] structure of sequence from [Mycobacterium tuberculosis] with ACT and THM as [ligands]. Active as [[1]], with EC number [2.7.4.9]. Full crystallographic information is available from [OCA].
ReferenceReference
The crystal structure of Mycobacterium tuberculosis thymidylate kinase in complex with 3'-azidodeoxythymidine monophosphate suggests a mechanism for competitive inhibition., Fioravanti E, Adam V, Munier-Lehmann H, Bourgeois D, Biochemistry. 2005 Jan 11;44(1):130-7. PMID:15628853
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