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| | <StructureSection load='2xvx' size='340' side='right'caption='[[2xvx]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='2xvx' size='340' side='right'caption='[[2xvx]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2xvx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Desvh Desvh]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XVX OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2XVX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2xvx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Desvh Desvh]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XVX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XVX FirstGlance]. <br> |
| | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CO2:CARBON+DIOXIDE'>CO2</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CO2:CARBON+DIOXIDE'>CO2</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Sirohydrochlorin_cobaltochelatase Sirohydrochlorin cobaltochelatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.99.1.3 4.99.1.3] </span></td></tr> | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Sirohydrochlorin_cobaltochelatase Sirohydrochlorin cobaltochelatase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.99.1.3 4.99.1.3] </span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2xvx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xvx OCA], [http://pdbe.org/2xvx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2xvx RCSB], [http://www.ebi.ac.uk/pdbsum/2xvx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2xvx 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=2xvx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xvx OCA], [https://pdbe.org/2xvx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xvx RCSB], [https://www.ebi.ac.uk/pdbsum/2xvx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xvx ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CBIKP_DESVH CBIKP_DESVH]] Catalyzes the insertion of Co(2+) into sirohydrochlorin. To a lesser extent, is also able to insert Fe(2+) into sirohydrochlorin, yielding siroheme. Its periplasmic location means that it cannot participate in cobalamin biosynthesis and its genomic environment suggests it is likely to be associated with a heme or metal transport system.<ref>PMID:18457416</ref> | + | [[https://www.uniprot.org/uniprot/CBIKP_DESVH CBIKP_DESVH]] Catalyzes the insertion of Co(2+) into sirohydrochlorin. To a lesser extent, is also able to insert Fe(2+) into sirohydrochlorin, yielding siroheme. Its periplasmic location means that it cannot participate in cobalamin biosynthesis and its genomic environment suggests it is likely to be associated with a heme or metal transport system.<ref>PMID:18457416</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Structural highlights
2xvx is a 1 chain structure with sequence from Desvh. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , , , , , |
| Activity: | Sirohydrochlorin cobaltochelatase, with EC number 4.99.1.3 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[CBIKP_DESVH] Catalyzes the insertion of Co(2+) into sirohydrochlorin. To a lesser extent, is also able to insert Fe(2+) into sirohydrochlorin, yielding siroheme. Its periplasmic location means that it cannot participate in cobalamin biosynthesis and its genomic environment suggests it is likely to be associated with a heme or metal transport system.[1]
Publication Abstract from PubMed
The class II chelatases associated with heme, siroheme, and cobalamin biosynthesis are structurally related enzymes that insert a specific metal ion (Fe(2+) or Co(2+)) into the center of a modified tetrapyrrole (protoporphyrin or sirohydrochlorin). The structures of two related class II enzymes, CbiX(S) from Archaeoglobus fulgidus and CbiK from Salmonella enterica, that are responsible for the insertion of cobalt along the cobalamin biosynthesis pathway are presented in complex with their metallated product. A further structure of a CbiK from Desulfovibrio vulgaris Hildenborough reveals how cobalt is bound at the active site. The crystal structures show that the binding of sirohydrochlorin is distinctly different to porphyrin binding in the protoporphyrin ferrochelatases and provide a molecular overview of the mechanism of chelation. The structures also give insights into the evolution of chelatase form and function. Finally, the structure of a periplasmic form of Desulfovibrio vulgaris Hildenborough CbiK reveals a novel tetrameric arrangement of its subunits that are stabilized by the presence of a heme b cofactor. Whereas retaining colbaltochelatase activity, this protein has acquired a central cavity with the potential to chaperone or transport metals across the periplasmic space, thereby evolving a new use for an ancient protein subunit.
Evolution in a family of chelatases facilitated by the introduction of active site asymmetry and protein oligomerization.,Romao CV, Ladakis D, Lobo SA, Carrondo MA, Brindley AA, Deery E, Matias PM, Pickersgill RW, Saraiva LM, Warren MJ Proc Natl Acad Sci U S A. 2010 Dec 20. PMID:21173279[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lobo SA, Brindley AA, Romao CV, Leech HK, Warren MJ, Saraiva LM. Two distinct roles for two functional cobaltochelatases (CbiK) in Desulfovibrio vulgaris hildenborough. Biochemistry. 2008 May 27;47(21):5851-7. doi: 10.1021/bi800342c. Epub 2008 May 6. PMID:18457416 doi:http://dx.doi.org/10.1021/bi800342c
- ↑ Romao CV, Ladakis D, Lobo SA, Carrondo MA, Brindley AA, Deery E, Matias PM, Pickersgill RW, Saraiva LM, Warren MJ. Evolution in a family of chelatases facilitated by the introduction of active site asymmetry and protein oligomerization. Proc Natl Acad Sci U S A. 2010 Dec 20. PMID:21173279 doi:10.1073/pnas.1014298108
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