2fr0

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[[Image:2fr0.gif|left|200px]]
 
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{{Structure
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==The first ketoreductase of the erythromycin synthase (crystal form 1)==
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|PDB= 2fr0 |SIZE=350|CAPTION= <scene name='initialview01'>2fr0</scene>, resolution 1.81&Aring;
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<StructureSection load='2fr0' size='340' side='right'caption='[[2fr0]], [[Resolution|resolution]] 1.81&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>
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<table><tr><td colspan='2'>[[2fr0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharopolyspora_erythraea Saccharopolyspora erythraea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FR0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FR0 FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/3-oxoacyl-[acyl-carrier-protein]_reductase 3-oxoacyl-[acyl-carrier-protein] reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.100 1.1.1.100] </span>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.81&#8491;</td></tr>
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|GENE= eryAI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1836 Saccharopolyspora erythraea])
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<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></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2fr0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fr0 OCA], [https://pdbe.org/2fr0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fr0 RCSB], [https://www.ebi.ac.uk/pdbsum/2fr0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fr0 ProSAT]</span></td></tr>
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|RELATEDENTRY=[[2fr1|2FR1]], [[2fro|2FRO]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fr0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fr0 OCA], [http://www.ebi.ac.uk/pdbsum/2fr0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2fr0 RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/ERYA1_SACER ERYA1_SACER]
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== Evolutionary Conservation ==
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'''The first ketoreductase of the erythromycin synthase (crystal form 1)'''
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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==Overview==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fr/2fr0_consurf.spt"</scriptWhenChecked>
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The structure of the ketoreductase (KR) from the first module of the erythromycin synthase with NADPH bound was solved to 1.79 A resolution. The 51 kDa domain has two subdomains, each similar to a short-chain dehydrogenase/reductase (SDR) monomer. One subdomain has a truncated Rossmann fold and serves a purely structural role stabilizing the other subdomain, which catalyzes the reduction of the beta-carbonyl of a polyketide and possibly the epimerization of an alpha-substituent. The structure enabled us to define the domain boundaries of KR, the dehydratase (DH), and the enoylreductase (ER). It also constrains the three-dimensional organization of these domains within a module, revealing that KR does not make dimeric contacts across the 2-fold axis of the module. The quaternary structure elucidates how substrates are shuttled between the active sites of polyketide synthases (PKSs), as well as related fatty acid synthases (FASs), and suggests how domains can be swapped to make hybrid synthases that produce novel polyketides.
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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==About this Structure==
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</jmolCheckbox>
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2FR0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharopolyspora_erythraea Saccharopolyspora erythraea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FR0 OCA].
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</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=2fr0 ConSurf].
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<div style="clear:both"></div>
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==Reference==
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__TOC__
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The structure of a ketoreductase determines the organization of the beta-carbon processing enzymes of modular polyketide synthases., Keatinge-Clay AT, Stroud RM, Structure. 2006 Apr;14(4):737-48. Epub 2006 Mar 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16564177 16564177]
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</StructureSection>
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[[Category: 3-oxoacyl-[acyl-carrier-protein] reductase]]
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[[Category: Large Structures]]
[[Category: Saccharopolyspora erythraea]]
[[Category: Saccharopolyspora erythraea]]
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[[Category: Single protein]]
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[[Category: Keatinge-Clay AT]]
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[[Category: Keatinge-Clay, A T.]]
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[[Category: Stroud RM]]
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[[Category: Stroud, R M.]]
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[[Category: short chain dehydrogenase/reductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:06:32 2008''
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Current revision

The first ketoreductase of the erythromycin synthase (crystal form 1)

PDB ID 2fr0

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