1j6q: Difference between revisions

Revision as of 14:33, 1 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:1j6q.png

Template:STRUCTURE 1j6q

Solution structure and characterization of the heme chaperone CcmESolution structure and characterization of the heme chaperone CcmE

Template:ABSTRACT PUBMED 12427019

About this StructureAbout this Structure

1J6Q is a Single protein structure of sequence from Shewanella putrefaciens. Full experimental information is available from OCA.

ReferenceReference

Solution structure and characterization of the heme chaperone CcmE., Arnesano F, Banci L, Barker PD, Bertini I, Rosato A, Su XC, Viezzoli MS, Biochemistry. 2002 Nov 19;41(46):13587-94. PMID:12427019

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-'''Solution structure and characterization of the heme chaperone CcmE'''
+===Solution structure and characterization of the heme chaperone CcmE===
-==Overview==
+<!--
-The covalent attachment of the heme cofactor in c-type cytochromes is a surprisingly complex process, which in bacteria involves a number of different proteins. Among the latter, the ccmE gene product is known to perform a key role in the heme delivery pathway in Gram-negative bacteria. The solution structure of the soluble domain of apo-CcmE from Shewanella putrefaciens was determined through NMR spectroscopy on a 13C,15N-labeled sample. The structure is characterized by a compact core with large regions of beta structure, while the N-terminal and C-terminal regions are essentially unstructured. The overall folding is similar to that of the so-called oligo-binding proteins (OB fold). Solvent-exposed aromatic residues, conserved in all CcmE homologues, have been found in the proximity of His131, the putative heme-binding residue, that could have a role in the interaction with heme. No interaction between CcmE and heme, as well as between CcmE and holocytochrome c, could be detected in vitro by electronic spectroscopy or by NMR. The data available suggest that the heme transfer process is likely to involve a heterooligomeric protein complex and occur under a tight enzymatic control.
+The line below this paragraph, {{ABSTRACT_PUBMED_12427019}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_12427019}}
 ==About this Structure==
-J6Q is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Shewanella_putrefaciens Shewanella putrefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J6Q OCA].
+J6Q is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Shewanella_putrefaciens Shewanella putrefaciens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J6Q OCA].
 ==Reference==
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 [[Category: All-beta protein]]
 [[Category: Heme delivery,cytochrome c maturation]]
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