1pdo: Difference between revisions

Revision as of 20:44, 27 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:1pdo.png

Template:STRUCTURE 1pdo

PHOSPHOENOLPYRUVATE-DEPENDENT PHOSPHOTRANSFERASE SYSTEMPHOSPHOENOLPYRUVATE-DEPENDENT PHOSPHOTRANSFERASE SYSTEM

Template:ABSTRACT PUBMED 8676384

About this StructureAbout this Structure

1PDO is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Structure of the IIA domain of the mannose transporter from Escherichia coli at 1.7 angstroms resolution., Nunn RS, Markovic-Housley Z, Genovesio-Taverne JC, Flukiger K, Rizkallah PJ, Jansonius JN, Schirmer T, Erni B, J Mol Biol. 1996 Jun 14;259(3):502-11. PMID:8676384

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1pdo.jpg|left|200px]]
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-'''PHOSPHOENOLPYRUVATE-DEPENDENT PHOSPHOTRANSFERASE SYSTEM'''
+===PHOSPHOENOLPYRUVATE-DEPENDENT PHOSPHOTRANSFERASE SYSTEM===
-==Overview==
+<!--
-The mannose transporter from Escherichia coli is a member of the phosphoenolpyruvate-dependent phosphotransferase system. The multi-subunit complex couples translocation across the bacterial inner membrane with phosphorylation of the solute. A functional fragment (IIA(Man), residues 2 to 133) of the membrane-associated IIAB(Man) subunit of the mannose transporter was expressed as a selenomethionine protein, and the unphosphorylated molecule was crystallized and its structure solved by X-ray crystallography. The protein consists of a central five-stranded beta-sheet covered by helices on either face. The order of the secondary structure elements is (beta alpha)4, alpha beta. Four beta-strands are arranged in a parallel manner with strand order 2134 and are linked by helices forming right-handed cross-over connections. The fifth strand that forms one edge of the sheet and runs antiparallel to the others is swapped between the subunits of the dimeric structure. Helices D and E form a helical hairpin. Histidine 10, which is transiently phosphorylated during catalysis, is located at the topological switch-point of the structure, close to the subunit interface. Its imidazole ring is hydrogen bonded to the buried side-chain of Asp67. It is likely that Asp67 acts as a general base and thus increases the nucleophilicity of the histidine. Modeling suggests that the covalently bound phosphoryl group would be stabilized by the macrodipole of helix C. Putative interactions between IIA(Man) and the histidine-containing phosphocarrier protein are discussed.
+The line below this paragraph, {{ABSTRACT_PUBMED_8676384}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 8676384 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_8676384}}
 ==About this Structure==
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 [[Category: Schirmer, T.]]
 [[Category: Phosphoenolpyruvate dependent phosphotransferase system]]
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