1j6q: Difference between revisions
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< | ==Solution structure and characterization of the heme chaperone CcmE== | ||
<StructureSection load='1j6q' size='340' side='right'caption='[[1j6q]]' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1j6q]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1J6Q FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | |||
-- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1j6q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j6q OCA], [https://pdbe.org/1j6q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1j6q RCSB], [https://www.ebi.ac.uk/pdbsum/1j6q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1j6q ProSAT]</span></td></tr> | ||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/CCME_SHEON CCME_SHEON] Heme chaperone required for the biogenesis of c-type cytochromes. Transiently binds heme delivered by CcmC and transfers the heme to apo-cytochromes in a process facilitated by CcmF and CcmH (By similarity). | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/j6/1j6q_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1j6q ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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<ref>PMID:12427019</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1j6q" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Large Structures]] | ||
== | |||
< | |||
[[Category: Shewanella putrefaciens]] | [[Category: Shewanella putrefaciens]] | ||
[[Category: Arnesano | [[Category: Arnesano F]] | ||
[[Category: Banci | [[Category: Banci L]] | ||
[[Category: Barker | [[Category: Barker PD]] | ||
[[Category: Bertini | [[Category: Bertini I]] | ||
[[Category: Rosato | [[Category: Rosato A]] | ||
[[Category: Su | [[Category: Su XC]] | ||
[[Category: Viezzoli | [[Category: Viezzoli MS]] | ||
Latest revision as of 11:36, 22 May 2024
Solution structure and characterization of the heme chaperone CcmESolution structure and characterization of the heme chaperone CcmE
Structural highlights
FunctionCCME_SHEON Heme chaperone required for the biogenesis of c-type cytochromes. Transiently binds heme delivered by CcmC and transfers the heme to apo-cytochromes in a process facilitated by CcmF and CcmH (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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