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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]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <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 [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1SR3 FirstGlance]. <br> | + | <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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CCME ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr> | + | </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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1sr3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sr3 OCA], [http://pdbe.org/1sr3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1sr3 RCSB], [http://www.ebi.ac.uk/pdbsum/1sr3 PDBsum], [http://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 == |
| - | [[http://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] | + | [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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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| - | [[Category: Enggist, E]] | + | [[Category: Large Structures]] |
| - | [[Category: Guntert, P]] | + | [[Category: Enggist E]] |
| - | [[Category: Pervushin, K]] | + | [[Category: Guntert P]] |
| - | [[Category: Thony-Meyer, L]] | + | [[Category: Pervushin K]] |
| - | [[Category: Beta barrel]]
| + | [[Category: Thony-Meyer L]] |
| - | [[Category: Chaperone]]
| + | |
| - | [[Category: Flexible c-terminal domain]]
| + | |
| - | [[Category: Ob fold]]
| + | |
| Structural highlights
Function
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
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Enggist E, Thony-Meyer L, Guntert P, Pervushin K. NMR structure of the heme chaperone CcmE reveals a novel functional motif. Structure. 2002 Nov;10(11):1551-7. PMID:12429096
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