3slk

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:51, 1 March 2024) (edit) (undo)
 
(2 intermediate revisions not shown.)
Line 1: Line 1:
 +
==Structure of ketoreductase and enoylreductase didomain from modular polyketide synthase==
==Structure of ketoreductase and enoylreductase didomain from modular polyketide synthase==
-
<StructureSection load='3slk' size='340' side='right' caption='[[3slk]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
+
<StructureSection load='3slk' size='340' side='right'caption='[[3slk]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[3slk]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharopolyspora_spinosa Saccharopolyspora spinosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SLK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SLK FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[3slk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharopolyspora_spinosa Saccharopolyspora spinosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SLK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SLK FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 3&#8491;</td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">spnB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=60894 Saccharopolyspora spinosa])</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-
<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=3slk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3slk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3slk RCSB], [http://www.ebi.ac.uk/pdbsum/3slk PDBsum]</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=3slk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3slk OCA], [https://pdbe.org/3slk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3slk RCSB], [https://www.ebi.ac.uk/pdbsum/3slk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3slk ProSAT]</span></td></tr>
</table>
</table>
-
<div style="background-color:#fffaf0;">
+
== Function ==
-
== Publication Abstract from PubMed ==
+
[https://www.uniprot.org/uniprot/Q9ALM5_SACSN Q9ALM5_SACSN]
-
The enoylreductase (ER) is the final common enzyme from modular polyketide synthases (PKSs) to be structurally characterized. The 3.0 A-resolution structure of the didomain comprising the ketoreductase (KR) and ER from the second module of the spinosyn PKS reveals that ER shares an approximately 600-A(2) interface with KR distinct from that of the related mammalian fatty acid synthase (FAS). In contrast to the ER domains of the mammalian FAS, the ER domains of the second module of the spinosyn PKS do not make contact across the two-fold axis of the synthase. This monomeric organization may have been necessary in the evolution of multimodular PKSs to enable acyl carrier proteins to access each of their cognate enzymes. The isolated ER domain showed activity toward a substrate analog, enabling us to determine the contributions of its active site residues.
+
-
 
+
-
Divergence of multimodular polyketide synthases revealed by a didomain structure.,Zheng J, Gay DC, Demeler B, White MA, Keatinge-Clay AT Nat Chem Biol. 2012 May 27. doi: 10.1038/nchembio.964. PMID:22634636<ref>PMID:22634636</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
== References ==
+
-
<references/>
+
__TOC__
__TOC__
</StructureSection>
</StructureSection>
 +
[[Category: Large Structures]]
[[Category: Saccharopolyspora spinosa]]
[[Category: Saccharopolyspora spinosa]]
-
[[Category: Gay, D C]]
+
[[Category: Gay DC]]
-
[[Category: Keatinge-Clay, A T]]
+
[[Category: Keatinge-Clay AT]]
-
[[Category: Zheng, J]]
+
[[Category: Zheng J]]
-
[[Category: Nadph]]
+
-
[[Category: Oxidoreductase]]
+
-
[[Category: Rossmann fold]]
+

Current revision

Structure of ketoreductase and enoylreductase didomain from modular polyketide synthase

PDB ID 3slk

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3slk"
Personal tools