1pzr: Difference between revisions

Revision as of 12:04, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1pzr.png

Template:STRUCTURE 1pzr

Structure of fused docking domains from the erythromycin polyketide synthase (DEBS), a model for the interaction between DEBS2 and DEBS3: the B domainStructure of fused docking domains from the erythromycin polyketide synthase (DEBS), a model for the interaction between DEBS2 and DEBS3: the B domain

Template:ABSTRACT PUBMED 12954331

About this StructureAbout this Structure

1PZR is a Single protein structure of sequence from Saccharopolyspora erythraea. Full experimental information is available from OCA.

ReferenceReference

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

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 {{STRUCTURE_1pzr|  PDB=1pzr  |  SCENE=  }}
-'''Structure of fused docking domains from the erythromycin polyketide synthase (DEBS), a model for the interaction between DEBS2 and DEBS3: the B domain'''
+===Structure of fused docking domains from the erythromycin polyketide synthase (DEBS), a model for the interaction between DEBS2 and DEBS3: the B domain===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_12954331}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12954331 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_12954331}}
 ==About this Structure==
-PZR 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=1PZR OCA].
+PZR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharopolyspora_erythraea Saccharopolyspora erythraea]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PZR OCA].
 ==Reference==
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 [[Category: Four helix bundle]]
 [[Category: Homodimer]]
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