2b7l

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Revision as of 19:18, 29 January 2008 by OCA (talk | contribs) (New page: left|200px<br /><applet load="2b7l" size="350" color="white" frame="true" align="right" spinBox="true" caption="2b7l, resolution 3.00Å" /> '''Crystal Structure of...)
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File:2b7l.gif


2b7l, resolution 3.00Å

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Crystal Structure of CTP:Glycerol-3-Phosphate Cytidylyltransferase from Staphylococcus aureus

OverviewOverview

Integrity of the cell wall is essential for bacterial survival, and as a, consequence components involved in its biosynthesis can potentially be, exploited as targets for antibiotics. One such potential target is, CTP:glycerol-3-phosphate cytidylyltransferase. This enzyme (TarD(Sa) in, Staphylococcus aureus and TagD(Bs) in Bacillus subtilis) catalyzes the, formation of CDP-glycerol, which is used for the assembly of linkages, between peptidoglycan and teichoic acid polymer in Gram-positive bacteria., Intriguingly, despite the high sequence identity between TarD(Sa) and, TagD(Bs) (69% identity), kinetic studies show that these two enzymes, differ markedly in their kinetic mechanism and activity. To examine the, basis for the disparate enzymological properties, we have determined the, crystal structure of TarD(Sa) in the apo state to 3 A resolution, and, performed equilibrium sedimentation analysis. Comparison of the structure, with that of CTP- and CDP-glycerol-bound TagD(Bs) crystal structures, reveals that the overall structure of TarD(Sa) is essentially the same as, that of TagD(Bs), except in the C-terminus, where it forms a helix in, TagD(Bs) but is disordered in the apo TarD(Sa) structure. In addition, TarD(Sa) can exist both as a tetramer and as a dimer, unlike TagD(Bs), which is a dimer. These observations shed light on the structural basis, for the differing kinetic characteristics between TarD(Sa) and TagD(Bs).

About this StructureAbout this Structure

2B7L is a Single protein structure of sequence from Staphylococcus aureus. Active as Glycerol-3-phosphate cytidylyltransferase, with EC number 2.7.7.39 Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of CTP:glycerol-3-phosphate cytidylyltransferase from Staphylococcus aureus: examination of structural basis for kinetic mechanism., Fong DH, Yim VC, D'Elia MA, Brown ED, Berghuis AM, Biochim Biophys Acta. 2006 Jan;1764(1):63-9. Epub 2005 Nov 10. PMID:16344011

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