8jfh: Difference between revisions
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==Crystal structure of 3-oxoacyl-ACP reductase FabG in complex with NADP+ and 3-keto-octanoyl-ACP from Helicobacter pylori in an inactive form that priors the acyl substrate delivery== | |||
<StructureSection load='8jfh' size='340' side='right'caption='[[8jfh]], [[Resolution|resolution]] 1.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8jfh]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8JFH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8JFH FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=PN7:N~3~-[(2S)-2-HYDROXY-3,3-DIMETHYL-4-(PHOSPHONOOXY)BUTANOYL]-N-(2-SULFANYLETHYL)-BETA-ALANINAMIDE'>PN7</scene>, <scene name='pdbligand=UHC:~{S}-[2-[3-[[(2~{S})-3,3-dimethyl-2-oxidanyl-4-phosphonooxy-butanoyl]amino]propanoylamino]ethyl]+3-oxidanylideneoctanethioate'>UHC</scene></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=8jfh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8jfh OCA], [https://pdbe.org/8jfh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8jfh RCSB], [https://www.ebi.ac.uk/pdbsum/8jfh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8jfh ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q5EDC8_HELPX Q5EDC8_HELPX] Carrier of the growing fatty acid chain in fatty acid biosynthesis.[HAMAP-Rule:MF_01217][RuleBase:RU003545][SAAS:SAAS00510058] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The short-chain dehydrogenase/reductase (SDR) superfamily members acyl-ACP reductases FabG and FabI are indispensable core enzymatic modules and catalytic orientation controllers in type-II fatty acid biosynthesis. Herein, we report their distinct substrate allosteric recognition and enantioselective reduction mechanisms. FabG achieves allosteric regulation of ACP and NADPH through ACP binding across two adjacent FabG monomers, while FabI follows an irreversible compulsory order of substrate binding in that NADH binding must precede that of ACP on a discrete FabI monomer. Moreover, FabG and FabI utilize a backdoor residue Phe187 or a "rheostat" alpha8 helix for acyl chain length selection, and their corresponding triad residues Ser142 or Tyr145 recognize the keto- or enoyl-acyl substrates, respectively, facilitating initiation of nucleophilic attack by NAD(P)H. The other two triad residues (Tyr and Lys) mediate subsequent proton transfer and (R)-3-hydroxyacyl- or saturated acyl-ACP production. | |||
The Molecular Basis of Catalysis by SDR Family Members Ketoacyl-ACP Reductase FabG and Enoyl-ACP Reductase FabI in Type-II Fatty Acid Biosynthesis.,Zhou J, Zhang L, Wang Y, Song W, Huang Y, Mu Y, Schmitz W, Zhang SY, Lin H, Chen HZ, Ye F, Zhang L Angew Chem Int Ed Engl. 2023 Nov 13;62(46):e202313109. doi: , 10.1002/anie.202313109. Epub 2023 Oct 12. PMID:37779101<ref>PMID:37779101</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 8jfh" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Helicobacter pylori]] | |||
[[Category: Large Structures]] | |||
[[Category: Zhang L]] | |||
[[Category: Zhou JS]] | |||
Latest revision as of 15:18, 23 October 2024
Crystal structure of 3-oxoacyl-ACP reductase FabG in complex with NADP+ and 3-keto-octanoyl-ACP from Helicobacter pylori in an inactive form that priors the acyl substrate deliveryCrystal structure of 3-oxoacyl-ACP reductase FabG in complex with NADP+ and 3-keto-octanoyl-ACP from Helicobacter pylori in an inactive form that priors the acyl substrate delivery
Structural highlights
FunctionQ5EDC8_HELPX Carrier of the growing fatty acid chain in fatty acid biosynthesis.[HAMAP-Rule:MF_01217][RuleBase:RU003545][SAAS:SAAS00510058] Publication Abstract from PubMedThe short-chain dehydrogenase/reductase (SDR) superfamily members acyl-ACP reductases FabG and FabI are indispensable core enzymatic modules and catalytic orientation controllers in type-II fatty acid biosynthesis. Herein, we report their distinct substrate allosteric recognition and enantioselective reduction mechanisms. FabG achieves allosteric regulation of ACP and NADPH through ACP binding across two adjacent FabG monomers, while FabI follows an irreversible compulsory order of substrate binding in that NADH binding must precede that of ACP on a discrete FabI monomer. Moreover, FabG and FabI utilize a backdoor residue Phe187 or a "rheostat" alpha8 helix for acyl chain length selection, and their corresponding triad residues Ser142 or Tyr145 recognize the keto- or enoyl-acyl substrates, respectively, facilitating initiation of nucleophilic attack by NAD(P)H. The other two triad residues (Tyr and Lys) mediate subsequent proton transfer and (R)-3-hydroxyacyl- or saturated acyl-ACP production. The Molecular Basis of Catalysis by SDR Family Members Ketoacyl-ACP Reductase FabG and Enoyl-ACP Reductase FabI in Type-II Fatty Acid Biosynthesis.,Zhou J, Zhang L, Wang Y, Song W, Huang Y, Mu Y, Schmitz W, Zhang SY, Lin H, Chen HZ, Ye F, Zhang L Angew Chem Int Ed Engl. 2023 Nov 13;62(46):e202313109. doi: , 10.1002/anie.202313109. Epub 2023 Oct 12. PMID:37779101[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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