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| | ==Crystal structure of FabG from Synechocystis sp. PCC 6803== | | ==Crystal structure of FabG from Synechocystis sp. PCC 6803== |
| - | <StructureSection load='4rzh' size='340' side='right' caption='[[4rzh]], [[Resolution|resolution]] 2.20Å' scene=''> | + | <StructureSection load='4rzh' size='340' side='right'caption='[[4rzh]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4rzh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aphanocapsa_sp._(strain_n-1) Aphanocapsa sp. (strain n-1)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RZH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RZH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4rzh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechocystis_sp._PCC_6803 Synechocystis sp. PCC 6803]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RZH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RZH FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4rzi|4rzi]]</td></tr> | + | </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=4rzh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rzh OCA], [https://pdbe.org/4rzh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rzh RCSB], [https://www.ebi.ac.uk/pdbsum/4rzh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rzh ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fabG, MYO_110490 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1148 Aphanocapsa sp. (strain N-1)])</td></tr>
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| - | <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=4rzh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rzh OCA], [http://pdbe.org/4rzh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4rzh RCSB], [http://www.ebi.ac.uk/pdbsum/4rzh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4rzh ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/FABG_SYNY3 FABG_SYNY3] Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis (Probable). Is capable of reducing acetoacetyl-CoA, but less well than its paralog PhaB (PubMed:26358291).<ref>PMID:26358291</ref> <ref>PMID:26358291</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: Liu, Y]] | + | [[Category: Large Structures]] |
| - | [[Category: Xue, S]] | + | [[Category: Synechocystis sp. PCC 6803]] |
| - | [[Category: Keto-acyl reductase]] | + | [[Category: Liu Y]] |
| - | [[Category: Oxidoreductase]] | + | [[Category: Xue S]] |
| Structural highlights
Function
FABG_SYNY3 Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis (Probable). Is capable of reducing acetoacetyl-CoA, but less well than its paralog PhaB (PubMed:26358291).[1] [2]
Publication Abstract from PubMed
PhaB (acetoacetyl-CoA reductase) catalyzes the reduction of acetoacetyl-CoA to (R)-3-hydroxybutyryl-CoA in polyhydroxybutyrate (PHB) synthesis and FabG (3-ketoacyl-acyl-carrier-protein reductase) catalyzes the beta-ketoacyl-ACP to yield (R)-3-hydroxyacyl-ACP in fatty acid biosynthesis. Both of them have been classified into the same group EC 1.1.1. PhaB is limited with substrate specificities, while FabG was considered as a potential PhaB due to broad substrate selectivity despite of low activity. Here, X-ray crystal structures of FabG and PhaB from the photosynthetic microorganism Synechocystis sp. PCC 6803 were resolved. Based on them, a high-performance FabG on acyl-CoA directed by structural evolution was constructed that may serve as a critical enzyme to partition carbon flow from fatty acid synthesis to PHA.
Structure-directed construction of a high-performance version of the enzyme FabG from the photosynthetic microorganism Synechocystis sp. PCC 6803.,Liu Y, Feng Y, Cao X, Li X, Xue S FEBS Lett. 2015 Sep 7. pii: S0014-5793(15)00815-7. doi:, 10.1016/j.febslet.2015.09.001. PMID:26358291[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Liu Y, Feng Y, Cao X, Li X, Xue S. Structure-directed construction of a high-performance version of the enzyme FabG from the photosynthetic microorganism Synechocystis sp. PCC 6803. FEBS Lett. 2015 Sep 7. pii: S0014-5793(15)00815-7. doi:, 10.1016/j.febslet.2015.09.001. PMID:26358291 doi:http://dx.doi.org/10.1016/j.febslet.2015.09.001
- ↑ Liu Y, Feng Y, Cao X, Li X, Xue S. Structure-directed construction of a high-performance version of the enzyme FabG from the photosynthetic microorganism Synechocystis sp. PCC 6803. FEBS Lett. 2015 Sep 7. pii: S0014-5793(15)00815-7. doi:, 10.1016/j.febslet.2015.09.001. PMID:26358291 doi:http://dx.doi.org/10.1016/j.febslet.2015.09.001
- ↑ Liu Y, Feng Y, Cao X, Li X, Xue S. Structure-directed construction of a high-performance version of the enzyme FabG from the photosynthetic microorganism Synechocystis sp. PCC 6803. FEBS Lett. 2015 Sep 7. pii: S0014-5793(15)00815-7. doi:, 10.1016/j.febslet.2015.09.001. PMID:26358291 doi:http://dx.doi.org/10.1016/j.febslet.2015.09.001
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