1w4z
From Proteopedia
(Difference between revisions)
| (28 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | [[Image:1w4z.gif|left|200px]]<br /> | ||
| - | <applet load="1w4z" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1w4z, resolution 2.50Å" /> | ||
| - | '''STRUCTURE OF ACTINORHODIN POLYKETIDE (ACTIII) REDUCTASE'''<br /> | ||
| - | == | + | ==Structure of actinorhodin polyketide (actIII) Reductase== |
| - | We have determined the 2.5 angstroms crystal structure of an active, tetrameric Streptomyces coelicolor type II polyketide ketoreductase | + | <StructureSection load='1w4z' size='340' side='right'caption='[[1w4z]], [[Resolution|resolution]] 2.50Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1w4z]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W4Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W4Z 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]] 2.5Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</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=1w4z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w4z OCA], [https://pdbe.org/1w4z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w4z RCSB], [https://www.ebi.ac.uk/pdbsum/1w4z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w4z ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ACT3_STRCO ACT3_STRCO] | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/w4/1w4z_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1w4z ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | We have determined the 2.5 angstroms crystal structure of an active, tetrameric Streptomyces coelicolor type II polyketide ketoreductase (actIII) with its bound cofactor, NADP+. This structure shows a Rossman dinucleotide binding fold characteristic of SDR enzymes. Of two subunits in the crystallographic asymmetric unit, one is closed around the active site. Formate is observed in the open subunit, indicating possible carbonyl binding sites of the polyketide intermediate. Unlike previous models we observe crystal contacts that may mimic the KR-ACP interactions that may drive active site opening. Based on these observations, we have constructed a model for ACP and polyketide binding. We propose that binding of ACP triggers a conformational change from the closed to the open, active form of the enzyme. The polyketide chain enters the active site and reduction occurs. The model also suggests a general mechanism for ACP recognition which is applicable to a range of protein families. | ||
| - | + | The crystal structure of the actIII actinorhodin polyketide reductase: proposed mechanism for ACP and polyketide binding.,Hadfield AT, Limpkin C, Teartasin W, Simpson TJ, Crosby J, Crump MP Structure. 2004 Oct;12(10):1865-75. PMID:15458634<ref>PMID:15458634</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: | + | <div class="pdbe-citations 1w4z" style="background-color:#fffaf0;"></div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Streptomyces coelicolor]] | [[Category: Streptomyces coelicolor]] | ||
| - | [[Category: Crosby | + | [[Category: Crosby J]] |
| - | [[Category: Crump | + | [[Category: Crump MP]] |
| - | [[Category: Hadfield | + | [[Category: Hadfield AT]] |
| - | [[Category: Limpkin | + | [[Category: Limpkin C]] |
| - | [[Category: Simpson | + | [[Category: Simpson TJ]] |
| - | [[Category: Teartasin | + | [[Category: Teartasin W]] |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
Structure of actinorhodin polyketide (actIII) Reductase
| |||||||||||
