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| <StructureSection load='5k1s' size='340' side='right'caption='[[5k1s]], [[Resolution|resolution]] 2.55Å' scene=''> | | <StructureSection load='5k1s' size='340' side='right'caption='[[5k1s]], [[Resolution|resolution]] 2.55Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[5k1s]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Myxxd Myxxd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K1S OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5K1S FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5k1s]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Myxococcus_xanthus_DK_1622 Myxococcus xanthus DK 1622]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K1S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5K1S FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.55Å</td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MXAN_4266 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=246197 MYXXD])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=5k1s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k1s OCA], [http://pdbe.org/5k1s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5k1s RCSB], [http://www.ebi.ac.uk/pdbsum/5k1s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5k1s 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=5k1s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k1s OCA], [https://pdbe.org/5k1s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5k1s RCSB], [https://www.ebi.ac.uk/pdbsum/5k1s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5k1s ProSAT]</span></td></tr> |
| </table> | | </table> |
| + | == Function == |
| + | [https://www.uniprot.org/uniprot/Q1D4I2_MYXXD Q1D4I2_MYXXD] |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| </StructureSection> | | </StructureSection> |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Myxxd]] | + | [[Category: Myxococcus xanthus DK 1622]] |
- | [[Category: Blankenfeldt, W]] | + | [[Category: Blankenfeldt W]] |
- | [[Category: Bock, T]] | + | [[Category: Bock T]] |
- | [[Category: Mueller, R]] | + | [[Category: Mueller R]] |
- | [[Category: Hexahistidine tag]]
| + | |
- | [[Category: Isovalerate]]
| + | |
- | [[Category: Medium chain reductase]]
| + | |
- | [[Category: Oxidoreductase]]
| + | |
- | [[Category: Tev-protease recognition sequence]]
| + | |
| Structural highlights
Function
Q1D4I2_MYXXD
Publication Abstract from PubMed
Isovaleryl coenzyme A (IV-CoA) performs a crucial role during development and fruiting-body formation in myxobacteria, which is reflected in the existence of a de novo biosynthetic pathway that is highly upregulated when leucine, the common precursor of IV-CoA, is limited. The final step in de novo IV-CoA biosynthesis is catalyzed by AibC, a medium-chain dehydrogenase/reductase. Here, the crystal structure of AibC from Myxococcus xanthus refined to 2.55 A resolution is presented. The protein adopts two different conformations in the crystal lattice, which is a consequence of partial interaction with the purification tag. Based on this structure, it is suggested that AibC most probably uses a Zn(2+)-supported catalytic mechanism in which NADPH is preferred over NADH. Taken together, this study reveals structural details of the alternative IV-CoA-producing pathway in myxobacteria, which may serve as a base for further biotechnological research and biofuel production.
Crystal structure of AibC, a reductase involved in alternative de novo isovaleryl coenzyme A biosynthesis in Myxococcus xanthus.,Bock T, Muller R, Blankenfeldt W Acta Crystallogr F Struct Biol Commun. 2016 Aug;72(Pt 8):652-8. doi:, 10.1107/S2053230X16011146. Epub 2016 Jul 29. PMID:27487931[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bock T, Muller R, Blankenfeldt W. Crystal structure of AibC, a reductase involved in alternative de novo isovaleryl coenzyme A biosynthesis in Myxococcus xanthus. Acta Crystallogr F Struct Biol Commun. 2016 Aug;72(Pt 8):652-8. doi:, 10.1107/S2053230X16011146. Epub 2016 Jul 29. PMID:27487931 doi:http://dx.doi.org/10.1107/S2053230X16011146
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