1pzr: Difference between revisions

Revision as of 15:34, 21 February 2008

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

OverviewOverview

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.

About this StructureAbout this Structure

1PZR is a Single protein structure of sequence from Saccharopolyspora erythraea. Active as Erythronolide synthase, with EC number 2.3.1.94 Full crystallographic 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

Page seeded by OCA on Thu Feb 21 14:34:18 2008

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OCA

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-[[Image:1pzr.gif|left|200px]]<br /><applet load="1pzr" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1pzr.gif|left|200px]]<br /><applet load="1pzr" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1pzr" />
 '''Structure of fused docking domains from the erythromycin polyketide synthase (DEBS), a model for the interaction between DEBS2 and DEBS3: the B domain'''<br />
 ==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.
+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.
 ==About this Structure==
-PZR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharopolyspora_erythraea Saccharopolyspora erythraea]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PZR OCA].
+PZR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharopolyspora_erythraea Saccharopolyspora erythraea]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PZR OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Saccharopolyspora erythraea]]
 [[Category: Single protein]]
-[[Category: Broadhurst, R.W.]]
+[[Category: Broadhurst, R W.]]
-[[Category: Leadlay, P.F.]]
+[[Category: Leadlay, P F.]]
 [[Category: Nietlispach, D.]]
-[[Category: Weissman, K.J.]]
+[[Category: Weissman, K J.]]
-[[Category: Wheatcroft, M.P.]]
+[[Category: Wheatcroft, M P.]]
 [[Category: four helix bundle]]
 [[Category: homodimer]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:15:55 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:34:18 2008''