3f5h

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[[Image:3f5h.jpg|left|200px]]
 
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==Crystal structure of fused docking domains from PikAIII and PikAIV of the pikromycin polyketide synthase==
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The line below this paragraph, containing "STRUCTURE_3f5h", creates the "Structure Box" on the page.
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<StructureSection load='3f5h' size='340' side='right'caption='[[3f5h]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3f5h]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_venezuelae Streptomyces venezuelae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3F5H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3F5H FirstGlance]. <br>
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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]] 1.75&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
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{{STRUCTURE_3f5h| PDB=3f5h | SCENE= }}
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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=3f5h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3f5h OCA], [https://pdbe.org/3f5h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3f5h RCSB], [https://www.ebi.ac.uk/pdbsum/3f5h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3f5h ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PIKA4_STRVZ PIKA4_STRVZ] Involved in the biosynthesis of 12- and 14-membered ring macrolactone antibiotics such as methymycin and neomethymycin, and pikromycin and narbomycin, respectively. Component of the pikromycin PKS which catalyzes the biosynthesis of both precursors 10-deoxymethynolide (12-membered ring macrolactone) and narbonolide (14-membered ring macrolactone). Chain elongation through PikAI, PikAII and PikAIII followed by thioesterase catalyzed termination results in the production of 10-deoxymethynolide, while continued elongation through PikAIV, followed by thioesterase (TE) catalyzed cyclization results in the biosynthesis of the narbonolide. The thioesterase can use a series of diketide-N-acetylcysteamine (SNAC) thioesters, but has a strong preference for the 2-methyl-3-ketopentanoyl-SNAC over the stereoisomers of 2-methyl-3-hydroxyacyl-SNAC (PubMed:12379101, PubMed:12733905).<ref>PMID:10421766</ref> <ref>PMID:10676969</ref> <ref>PMID:12379101</ref> <ref>PMID:12733905</ref> <ref>PMID:16969372</ref> <ref>PMID:17719493</ref> <ref>PMID:19027305</ref> [https://www.uniprot.org/uniprot/PIKA3_STRVZ PIKA3_STRVZ] Involved in the biosynthesis of 12- and 14-membered ring macrolactone antibiotics such as methymycin and neomethymycin, and pikromycin and narbomycin, respectively. Component of the pikromycin PKS which catalyzes the biosynthesis of both precursors 10-deoxymethynolide (12-membered ring macrolactone) and narbonolide (14-membered ring macrolactone). Chain elongation through PikAI, PikAII and PikAIII followed by thioesterase catalyzed termination results in the production of 10-deoxymethynolide, while continued elongation through PikAIV, followed by thioesterase (TE) catalyzed cyclization results in the biosynthesis of the narbonolide.<ref>PMID:10421766</ref> <ref>PMID:24965656</ref> <ref>PMID:19027305</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Bacterial type I polyketide synthases (PKSs) assemble structurally diverse natural products of significant clinical value from simple metabolic building blocks. The synthesis of these compounds occurs in a processive fashion along a large multiprotein complex. Transfer of the acyl intermediate across interpolypeptide junctions is mediated, at least in large part, by N- and C-terminal docking domains. We report here a comprehensive analysis of the binding affinity and selectivity for the complete set of discrete docking domain pairs in the pikromycin and erythromycin PKS systems. Despite disconnection from their parent module, each cognate pair of docking domains retained exquisite binding selectivity. Further insights were obtained by X-ray crystallographic analysis of the PikAIII/PikAIV docking domain interface. This new information revealed a series of key interacting residues that enabled development of a structural model for the recently proposed H2-T2 class of polypeptides involved in PKS intermodular molecular recognition.
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===Crystal structure of fused docking domains from PikAIII and PikAIV of the pikromycin polyketide synthase===
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Structural basis for binding specificity between subclasses of modular polyketide synthase docking domains.,Buchholz TJ, Geders TW, Bartley FE 3rd, Reynolds KA, Smith JL, Sherman DH ACS Chem Biol. 2009 Jan 16;4(1):41-52. PMID:19146481<ref>PMID:19146481</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 3f5h" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 19146481 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_19146481}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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3F5H is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Streptomyces_venezuelae Streptomyces venezuelae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3F5H OCA].
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==Reference==
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<ref group="xtra">PMID:19146481</ref><references group="xtra"/>
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[[Category: Streptomyces venezuelae]]
[[Category: Streptomyces venezuelae]]
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[[Category: Bartley, F E.]]
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[[Category: Bartley FE]]
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[[Category: Buchholz, T J.]]
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[[Category: Buchholz TJ]]
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[[Category: Geders, T W.]]
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[[Category: Geders TW]]
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[[Category: Reynolds, K A.]]
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[[Category: Reynolds KA]]
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[[Category: Sherman, D H.]]
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[[Category: Sherman DH]]
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[[Category: Smith, J L.]]
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[[Category: Smith JL]]
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[[Category: Docking domain]]
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[[Category: H2-t2]]
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[[Category: Pikromycin]]
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[[Category: Polyketide synthase]]
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[[Category: Protein binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 28 09:54:45 2009''
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Current revision

Crystal structure of fused docking domains from PikAIII and PikAIV of the pikromycin polyketide synthase

PDB ID 3f5h

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