1sr3
From Proteopedia
(Difference between revisions)
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==Solution structure of the heme chaperone CcmE of Escherichia coli== | ==Solution structure of the heme chaperone CcmE of Escherichia coli== | ||
| - | <StructureSection load='1sr3' size='340' side='right'caption='[[1sr3 | + | <StructureSection load='1sr3' size='340' side='right'caption='[[1sr3]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1sr3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <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=' | + | </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> | <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> | </table> | ||
== Function == | == 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</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]. | </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]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == 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. | ||
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| - | 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> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1sr3" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Escherichia coli]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Enggist | + | [[Category: Enggist E]] |
| - | [[Category: Guntert | + | [[Category: Guntert P]] |
| - | [[Category: Pervushin | + | [[Category: Pervushin K]] |
| - | [[Category: Thony-Meyer | + | [[Category: Thony-Meyer L]] |
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Revision as of 08:34, 1 May 2024
Solution structure of the heme chaperone CcmE of Escherichia coli
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