8jfj
From Proteopedia
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(Replacing page with ''''Unreleased structure''' The entry 8jfj is ON HOLD until Paper Publication Authors: Description: Category: Unreleased Structures') |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of enoyl-ACP reductase FabI from Helicobacter pylori== | |
| + | <StructureSection load='8jfj' size='340' side='right'caption='[[8jfj]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8jfj]] 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=8JFJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8JFJ 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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8jfj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8jfj OCA], [https://pdbe.org/8jfj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8jfj RCSB], [https://www.ebi.ac.uk/pdbsum/8jfj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8jfj ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A086RSH0_HELPX A0A086RSH0_HELPX] | ||
| + | <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 8jfj" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Helicobacter pylori]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Song WY]] | ||
| + | [[Category: Zhang L]] | ||
Current revision
Crystal structure of enoyl-ACP reductase FabI from Helicobacter pylori
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