View source for 1sr3


==Solution structure of the heme chaperone CcmE of Escherichia coli==
<StructureSection load='1sr3' size='340' side='right'caption='[[1sr3]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1sr3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1liz 1liz]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SR3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SR3 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=1sr3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sr3 OCA], [https://pdbe.org/1sr3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sr3 RCSB], [https://www.ebi.ac.uk/pdbsum/1sr3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sr3 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CCME_ECOLI CCME_ECOLI] 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.[HAMAP-Rule:MF_01959]
== 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/sr/1sr3_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=1sr3 ConSurf].
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== Publication Abstract from PubMed ==
The concept of metal chaperones involves transient binding of metallic cofactors by specific proteins for delivery to enzymes in which they function. Metal chaperones thus provide a protective, as well as a transport, function. We report the first structure of a heme chaperone, CcmE, which comprises these two functions. We propose that the covalent attachment of heme to an exposed histidine occurs after heme binding at the surface of a rigid molecule with a flexible C-terminal domain. CcmE belongs to a family of proteins with a specific fold, which all share a function in delivery of specific molecular cargo.

NMR structure of the heme chaperone CcmE reveals a novel functional motif.,Enggist E, Thony-Meyer L, Guntert P, Pervushin K Structure. 2002 Nov;10(11):1551-7. PMID:12429096<ref>PMID:12429096</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 1sr3" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Enggist E]]
[[Category: Guntert P]]
[[Category: Pervushin K]]
[[Category: Thony-Meyer L]]