1j6q: Difference between revisions

Revision as of 14:19, 21 February 2008

Solution structure and characterization of the heme chaperone CcmE

OverviewOverview

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.

About this StructureAbout this Structure

1J6Q is a Single protein structure of sequence from Shewanella putrefaciens. Full crystallographic 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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-[[Image:1j6q.jpg|left|200px]]<br /><applet load="1j6q" size="450" color="white" frame="true" align="right" spinBox="true"
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 caption="1j6q" />
 '''Solution structure and characterization of the heme chaperone CcmE'''<br />
 ==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 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.
 ==About this Structure==
-J6Q is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Shewanella_putrefaciens Shewanella putrefaciens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1J6Q OCA].
+J6Q is a [http://en.wikipedia.org/wiki/Single_protein 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].
 ==Reference==
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 [[Category: Arnesano, F.]]
 [[Category: Banci, L.]]
-[[Category: Barker, P.D.]]
+[[Category: Barker, P D.]]
 [[Category: Bertini, I.]]
 [[Category: Rosato, A.]]
-[[Category: Su, X.C.]]
+[[Category: Su, X C.]]
-[[Category: Viezzoli, M.S.]]
+[[Category: Viezzoli, M S.]]
 [[Category: all-beta protein]]
 [[Category: cytochrome c maturation]]
@@ Line 25: / Line 25: @@
 [[Category: ob-(oligonucleotide binding)fold]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:58:07 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:19:17 2008''