2ju2

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{{STRUCTURE_2ju2| PDB=2ju2 | SCENE= }}
{{STRUCTURE_2ju2| PDB=2ju2 | SCENE= }}
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'''Minimized mean solution structure of the acyl carrier protein domain from module 2 of 6-deoxyerythronolide B synthase (DEBS)'''
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===Minimized mean solution structure of the acyl carrier protein domain from module 2 of 6-deoxyerythronolide B synthase (DEBS)===
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==Overview==
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Polyketides are a medicinally important class of natural products. The architecture of modular polyketide synthases (PKSs), composed of multiple covalently linked domains grouped into modules, provides an attractive framework for engineering novel polyketide-producing assemblies. However, impaired domain-domain interactions can compromise the efficiency of engineered polyketide biosynthesis. To facilitate the study of these domain-domain interactions, we have used nuclear magnetic resonance (NMR) spectroscopy to determine the first solution structure of an acyl carrier protein (ACP) domain from a modular PKS, 6-deoxyerythronolide B synthase (DEBS). The tertiary fold of this 10-kD domain is a three-helical bundle; an additional short helix in the second loop also contributes to the core helical packing. Superposition of residues 14-94 of the ensemble on the mean structure yields an average atomic RMSD of 0.64 +/- 0.09 Angstrom for the backbone atoms (1.21 +/- 0.13 Angstrom for all non-hydrogen atoms). The three major helices superimpose with a backbone RMSD of 0.48 +/- 0.10 Angstrom (0.99 +/- 0.11 Angstrom for non-hydrogen atoms). Based on this solution structure, homology models were constructed for five other DEBS ACP domains. Comparison of their steric and electrostatic surfaces at the putative interaction interface (centered on helix II) suggests a model for protein-protein recognition of ACP domains, consistent with the previously observed specificity. Site-directed mutagenesis experiments indicate that two of the identified residues influence the specificity of ACP recognition.
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{{ABSTRACT_PUBMED_17893358}}
==About this Structure==
==About this Structure==
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2JU2 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=2JU2 OCA].
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2JU2 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=2JU2 OCA].
==Reference==
==Reference==
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[[Category: Phosphopantetheine]]
[[Category: Phosphopantetheine]]
[[Category: Transferase]]
[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:17:16 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 19:15:49 2008''

Revision as of 16:15, 27 July 2008

Image:2ju2.png

Template:STRUCTURE 2ju2

Minimized mean solution structure of the acyl carrier protein domain from module 2 of 6-deoxyerythronolide B synthase (DEBS)

Template:ABSTRACT PUBMED 17893358

About this Structure

2JU2 is a Single protein structure of sequence from Saccharopolyspora erythraea. Full experimental information is available from OCA.

Reference

Solution structure and proposed domain domain recognition interface of an acyl carrier protein domain from a modular polyketide synthase., Alekseyev VY, Liu CW, Cane DE, Puglisi JD, Khosla C, Protein Sci. 2007 Oct;16(10):2093-107. PMID:17893358

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