2oq3: Difference between revisions

Revision as of 15:28, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2oq3.png

Template:STRUCTURE 2oq3

Solution Structure of the mannitol- specific cryptic phosphotransferase enzyme IIA CmtB from Escherichia coliSolution Structure of the mannitol- specific cryptic phosphotransferase enzyme IIA CmtB from Escherichia coli

Template:ABSTRACT PUBMED 17803963

About this StructureAbout this Structure

2OQ3 is a Single protein structure of sequence from Escherichia coli. Full experimental 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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-'''Solution Structure of the mannitol- specific cryptic phosphotransferase enzyme IIA CmtB from Escherichia coli'''
+===Solution Structure of the mannitol- specific cryptic phosphotransferase enzyme IIA CmtB from Escherichia coli===
-==Overview==
+<!--
-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 (IIAMtl) 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 IIAMtl. Further, the essential arginine residue at the active site of IIAMtl 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.
+The line below this paragraph, {{ABSTRACT_PUBMED_17803963}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17803963 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_17803963}}
 ==About this Structure==
-OQ3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OQ3 OCA].
+OQ3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OQ3 OCA].
 ==Reference==
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 [[Category: Phosphotransferase]]
 [[Category: Solution structure]]
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