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| | <StructureSection load='4xc7' size='340' side='right'caption='[[4xc7]], [[Resolution|resolution]] 3.45Å' scene=''> | | <StructureSection load='4xc7' size='340' side='right'caption='[[4xc7]], [[Resolution|resolution]] 3.45Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4xc7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Cupmc Cupmc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XC7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XC7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4xc7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Cupriavidus_metallidurans_CH34 Cupriavidus metallidurans CH34]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XC7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XC7 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BCO:BUTYRYL+COENZYME+A'>BCO</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BCO:BUTYRYL+COENZYME+A'>BCO</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4xc6|4xc6]], [[4xc8|4xc8]]</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=4xc7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xc7 OCA], [https://pdbe.org/4xc7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xc7 RCSB], [https://www.ebi.ac.uk/pdbsum/4xc7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xc7 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sbm, Rmet_0210 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=266264 CUPMC])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Isobutyryl-CoA_mutase Isobutyryl-CoA mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.13 5.4.99.13] </span></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=4xc7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xc7 OCA], [http://pdbe.org/4xc7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xc7 RCSB], [http://www.ebi.ac.uk/pdbsum/4xc7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4xc7 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/ICMF_CUPMC ICMF_CUPMC] Catalyzes the reversible interconversion of isobutyryl-CoA and n-butyryl-CoA, and to a much lesser extent, of pivalyl-CoA and isovaleryl-CoA, using radical chemistry (PubMed:22167181). Also exhibits GTPase activity, associated with its G-protein domain (MeaI) that functions as a chaperone that assists cofactor delivery and proper holo-enzyme assembly (PubMed:22167181, PubMed:25675500). The G-domain of IcmF has also a role in its cofactor repair (PubMed:28130442). Does not display ATPase activity.<ref>PMID:22167181</ref> <ref>PMID:25675500</ref> <ref>PMID:28130442</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Cupmc]] | + | [[Category: Cupriavidus metallidurans CH34]] |
| - | [[Category: Isobutyryl-CoA mutase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Drennan, C L]] | + | [[Category: Drennan CL]] |
| - | [[Category: Jost, M]] | + | [[Category: Jost M]] |
| - | [[Category: Complex]]
| + | |
| - | [[Category: G-protein chaperone]]
| + | |
| - | [[Category: Isomerase]]
| + | |
| - | [[Category: Radical enzyme]]
| + | |
| Structural highlights
Function
ICMF_CUPMC Catalyzes the reversible interconversion of isobutyryl-CoA and n-butyryl-CoA, and to a much lesser extent, of pivalyl-CoA and isovaleryl-CoA, using radical chemistry (PubMed:22167181). Also exhibits GTPase activity, associated with its G-protein domain (MeaI) that functions as a chaperone that assists cofactor delivery and proper holo-enzyme assembly (PubMed:22167181, PubMed:25675500). The G-domain of IcmF has also a role in its cofactor repair (PubMed:28130442). Does not display ATPase activity.[1] [2] [3]
Publication Abstract from PubMed
G-protein metallochaperones ensure fidelity during cofactor assembly for a variety of metalloproteins, including adenosylcobalamin (AdoCbl)-dependent methylmalonyl-CoA mutase and hydrogenase, and thus have both medical and biofuel development applications. Here, we present crystal structures of IcmF, a natural fusion protein of AdoCbl-dependent isobutyryl-CoA mutase and its corresponding G-protein chaperone, which reveal the molecular architecture of a G-protein metallochaperone in complex with its target protein. These structures show that conserved G-protein elements become ordered upon target protein association, creating the molecular pathways that both sense and report on the cofactor loading state. Structures determined of both apo- and holo-forms of IcmF depict both open and closed enzyme states, in which the cofactor-binding domain is alternatively positioned for cofactor loading and for catalysis. Notably, the G protein moves as a unit with the cofactor-binding domain, providing a visualization of how a chaperone assists in the sequestering of a precious cofactor inside an enzyme active site.
Visualization of a radical B12 enzyme with its G-protein chaperone.,Jost M, Cracan V, Hubbard PA, Banerjee R, Drennan CL Proc Natl Acad Sci U S A. 2015 Feb 24;112(8):2419-24. doi:, 10.1073/pnas.1419582112. Epub 2015 Feb 9. PMID:25675500[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Cracan V, Banerjee R. Novel coenzyme B12-dependent interconversion of isovaleryl-CoA and pivalyl-CoA. J Biol Chem. 2012 Feb 3;287(6):3723-32. PMID:22167181 doi:10.1074/jbc.M111.320051
- ↑ Jost M, Cracan V, Hubbard PA, Banerjee R, Drennan CL. Visualization of a radical B12 enzyme with its G-protein chaperone. Proc Natl Acad Sci U S A. 2015 Feb 24;112(8):2419-24. doi:, 10.1073/pnas.1419582112. Epub 2015 Feb 9. PMID:25675500 doi:http://dx.doi.org/10.1073/pnas.1419582112
- ↑ Li Z, Kitanishi K, Twahir UT, Cracan V, Chapman D, Warncke K, Banerjee R. Cofactor Editing by the G-protein Metallochaperone Domain Regulates the Radical B(12) Enzyme IcmF. J Biol Chem. 2017 Mar 10;292(10):3977-3987. PMID:28130442 doi:10.1074/jbc.M117.775957
- ↑ Jost M, Cracan V, Hubbard PA, Banerjee R, Drennan CL. Visualization of a radical B12 enzyme with its G-protein chaperone. Proc Natl Acad Sci U S A. 2015 Feb 24;112(8):2419-24. doi:, 10.1073/pnas.1419582112. Epub 2015 Feb 9. PMID:25675500 doi:http://dx.doi.org/10.1073/pnas.1419582112
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