1pzq

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[[Image:1pzq.gif|left|200px]]
 
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{{Structure
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==Structure of fused docking domains from the erythromycin polyketide synthase (DEBS), a model for the interaction between DEBS 2 and DEBS 3: The A domain==
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|PDB= 1pzq |SIZE=350|CAPTION= <scene name='initialview01'>1pzq</scene>
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<StructureSection load='1pzq' size='340' side='right'caption='[[1pzq]]' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1pzq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharopolyspora_erythraea Saccharopolyspora erythraea]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PZQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PZQ FirstGlance]. <br>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Erythronolide_synthase Erythronolide synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.94 2.3.1.94]
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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|GENE= ERYA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1836 Saccharopolyspora erythraea])
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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=1pzq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pzq OCA], [https://pdbe.org/1pzq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pzq RCSB], [https://www.ebi.ac.uk/pdbsum/1pzq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pzq ProSAT]</span></td></tr>
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}}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ERYA2_SACER ERYA2_SACER]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Polyketides from actinomycete bacteria provide the basis for many valuable medicines, so engineering genes for their biosynthesis to produce variant molecules holds promise for drug discovery. The modular polyketide synthases are particularly amenable to this approach, because each cycle of chain extension is catalyzed by a different module of enzymes, and the modules are arranged within giant multienzyme subunits in the order in which they act. Protein-protein interactions between terminal docking domains of successive multienzymes promote their correct positioning within the assembly line, but because the overall complex is not stable in vitro, the key interactions have not been identified. We present here the NMR solution structure of a 120 residue polypeptide representing a typical pair of such domains, fused at their respective C and N termini: it adopts a stable dimeric structure which reveals the detailed role of these (predominantly helical) domains in docking and dimerization by modular polyketide synthases.
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'''Structure of fused docking domains from the erythromycin polyketide synthase (DEBS), a model for the interaction between DEBS 2 and DEBS 3: The A domain'''
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The structure of docking domains in modular polyketide synthases.,Broadhurst RW, Nietlispach D, Wheatcroft MP, Leadlay PF, Weissman KJ Chem Biol. 2003 Aug;10(8):723-31. PMID:12954331<ref>PMID:12954331</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>
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<div class="pdbe-citations 1pzq" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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Polyketides from actinomycete bacteria provide the basis for many valuable medicines, so engineering genes for their biosynthesis to produce variant molecules holds promise for drug discovery. The modular polyketide synthases are particularly amenable to this approach, because each cycle of chain extension is catalyzed by a different module of enzymes, and the modules are arranged within giant multienzyme subunits in the order in which they act. Protein-protein interactions between terminal docking domains of successive multienzymes promote their correct positioning within the assembly line, but because the overall complex is not stable in vitro, the key interactions have not been identified. We present here the NMR solution structure of a 120 residue polypeptide representing a typical pair of such domains, fused at their respective C and N termini: it adopts a stable dimeric structure which reveals the detailed role of these (predominantly helical) domains in docking and dimerization by modular polyketide synthases.
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*[[6-deoxyerythronolide B synthase 3D structures|6-deoxyerythronolide B synthase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1PZQ 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=1PZQ OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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The structure of docking domains in modular polyketide synthases., Broadhurst RW, Nietlispach D, Wheatcroft MP, Leadlay PF, Weissman KJ, Chem Biol. 2003 Aug;10(8):723-31. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12954331 12954331]
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[[Category: Erythronolide synthase]]
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[[Category: Saccharopolyspora erythraea]]
[[Category: Saccharopolyspora erythraea]]
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[[Category: Single protein]]
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[[Category: Broadhurst RW]]
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[[Category: Broadhurst, R W.]]
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[[Category: Leadlay PF]]
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[[Category: Leadlay, P F.]]
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[[Category: Nietlispach D]]
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[[Category: Nietlispach, D.]]
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[[Category: Weissman KJ]]
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[[Category: Weissman, K J.]]
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[[Category: Wheatcroft MP]]
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[[Category: Wheatcroft, M P.]]
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[[Category: four helix bundle]]
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[[Category: homodimer]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:31:09 2008''
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Current revision

Structure of fused docking domains from the erythromycin polyketide synthase (DEBS), a model for the interaction between DEBS 2 and DEBS 3: The A domain

PDB ID 1pzq

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