2b7l: Difference between revisions

Revision as of 07:56, 29 July 2008

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File:2b7l.png

Template:STRUCTURE 2b7l

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

Template:ABSTRACT PUBMED 16344011

About this StructureAbout this Structure

2B7L is a Single protein structure of sequence from Staphylococcus aureus. 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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-'''Crystal Structure of CTP:Glycerol-3-Phosphate Cytidylyltransferase from Staphylococcus aureus'''
+===Crystal Structure of CTP:Glycerol-3-Phosphate Cytidylyltransferase from Staphylococcus aureus===
-==Overview==
+<!--
-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).
+The line below this paragraph, {{ABSTRACT_PUBMED_16344011}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16344011 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_16344011}}
 ==About this Structure==
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 [[Category: Cytidylyltransferase]]
 [[Category: Rossmann fold]]
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