4rzh: Difference between revisions

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'''Unreleased structure'''


The entry 4rzh is ON HOLD
==Crystal structure of FabG from Synechocystis sp. PCC 6803==
<StructureSection load='4rzh' size='340' side='right'caption='[[4rzh]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</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>
</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;">
== 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.


Authors: Liu, Y., Xue, S.
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<ref>PMID:26358291</ref>


Description: Crystal structure of FabG from Synechocystis sp. PCC 6803
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Liu, Y]]
<div class="pdbe-citations 4rzh" style="background-color:#fffaf0;"></div>
[[Category: Xue, S]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Synechocystis sp. PCC 6803]]
[[Category: Liu Y]]
[[Category: Xue S]]
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