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| ==Glutaconyl-coA decarboxylase A subunit from Clostridium symbiosum co-crystallized with glutaconyl-coA== | | ==Glutaconyl-coA decarboxylase A subunit from Clostridium symbiosum co-crystallized with glutaconyl-coA== |
- | <StructureSection load='3gf3' size='340' side='right' caption='[[3gf3]], [[Resolution|resolution]] 1.75Å' scene=''> | + | <StructureSection load='3gf3' size='340' side='right'caption='[[3gf3]], [[Resolution|resolution]] 1.75Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[3gf3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacteroides_symbiosus"_stevens_1956 "bacteroides symbiosus" stevens 1956]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GF3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3GF3 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3gf3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_symbiosum Clostridium symbiosum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GF3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GF3 FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=COO:CROTONYL+COENZYME+A'>COO</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75Å</td></tr> |
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3gf7|3gf7]], [[3gma|3gma]], [[3glm|3glm]]</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=COO:CROTONYL+COENZYME+A'>COO</scene></td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gcdA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1512 "Bacteroides symbiosus" Stevens 1956])</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=3gf3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gf3 OCA], [https://pdbe.org/3gf3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3gf3 RCSB], [https://www.ebi.ac.uk/pdbsum/3gf3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3gf3 ProSAT]</span></td></tr> |
- | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutaconyl-CoA_decarboxylase Glutaconyl-CoA decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.70 4.1.1.70] </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=3gf3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gf3 OCA], [http://pdbe.org/3gf3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3gf3 RCSB], [http://www.ebi.ac.uk/pdbsum/3gf3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3gf3 ProSAT]</span></td></tr> | + | |
| </table> | | </table> |
| + | == Function == |
| + | [https://www.uniprot.org/uniprot/B7TVP1_CLOSY B7TVP1_CLOSY] |
| == 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: Bacteroides symbiosus stevens 1956]] | + | [[Category: Large Structures]] |
- | [[Category: Glutaconyl-CoA decarboxylase]]
| + | [[Category: Brugel D]] |
- | [[Category: Brugel, D]] | + | [[Category: Buckel W]] |
- | [[Category: Buckel, W]] | + | [[Category: Essen L-O]] |
- | [[Category: Essen, L O]] | + | [[Category: Kress D]] |
- | [[Category: Kress, D]] | + | |
- | [[Category: Biotin]]
| + | |
- | [[Category: Glutaconyl-coa decarboxylase]]
| + | |
- | [[Category: Glutamate fermentation]]
| + | |
- | [[Category: Lyase]]
| + | |
- | [[Category: Sodium ion transport]]
| + | |
| Structural highlights
Function
B7TVP1_CLOSY
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
Glutaconyl-CoA decarboxylase (Gcd) couples the biotin-dependent decarboxylation of glutaconyl-CoA with the generation of an electrochemical Na(+) gradient. Sequencing of the genes encoding all subunits of the Clostridium symbiosum decarboxylase membrane complex revealed that it comprises two distinct biotin carrier subunits, GcdC(1) and GcdC(2), which differ in the length of a central alanine- and proline-rich linker domain. Co-crystallization of the decarboxylase subunit GcdA with the substrate glutaconyl-CoA, the product crotonyl-CoA, and the substrate analogue glutaryl-CoA, respectively, resulted in a high resolution model for substrate binding and catalysis revealing remarkable structural changes upon substrate binding. Unlike the GcdA structure from Acidaminococcus fermentans, these data suggest that in intact Gcd complexes, GcdA is associated as a tetramer crisscrossed by a network of solvent-filled tunnels.
An asymmetric model for Na+-translocating glutaconyl-CoA decarboxylases.,Kress D, Brugel D, Schall I, Linder D, Buckel W, Essen LO J Biol Chem. 2009 Oct 9;284(41):28401-9. Epub 2009 Aug 4. PMID:19654317[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kress D, Brugel D, Schall I, Linder D, Buckel W, Essen LO. An asymmetric model for Na+-translocating glutaconyl-CoA decarboxylases. J Biol Chem. 2009 Oct 9;284(41):28401-9. Epub 2009 Aug 4. PMID:19654317 doi:10.1074/jbc.M109.037762
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