2oq3
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Solution Structure of the mannitol- specific cryptic phosphotransferase enzyme IIA CmtB from Escherichia coli
OverviewOverview
The bacterial phosphoenolpyruvate-dependent sugar phosphotransferase, system (PEP-PTS) is essential in the coupled transportation and, phosphorylation of various types of carbohydrates. The CmtAB proteins of, Escherichia coli are sequentially similar to the mannitol-specific, phosphotransferase MtlA. The CmtB protein corresponds to the, phosphotransferase enzyme IIA component. Here we report the solution, structure of CmtB from E. coli at high resolution by NMR spectroscopy. The, results show that CmtB adopts a globular fold consisting of a central, mixed five-strand beta-sheet flanked by seven helices at both sides., Structural comparison with the IIA domain of MtlA (IIA(Mtl)) reveals high, overall similarity, while notable conformational differences at the active, site are observed. The active site pocket of CmtB appears to be wider, and, the hydrophobic regions around it is larger compared to IIA(Mtl). Further, the essential arginine residue at the active site of IIA(Mtl) is, substituted by a serine in CmtB. Instead, the active pocket of CmtB, contains another arginine at a distinct position, suggesting different, molecular mechanisms for phosphoryl transfer.
About this StructureAbout this Structure
2OQ3 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
Solution structure of the cryptic mannitol-specific phosphotransferase enzyme IIA CmtB from Escherichia coli., Yu C, Li Y, Xia B, Jin C, Biochem Biophys Res Commun. 2007 Nov 3;362(4):1001-6. Epub 2007 Aug 27. PMID:17803963
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