2ju1

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|SITE=
|SITE=
|LIGAND=
|LIGAND=
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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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|ACTIVITY= <span class='plainlinks'>[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] </span>
|GENE= eryA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1836 Saccharopolyspora erythraea])
|GENE= eryA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1836 Saccharopolyspora erythraea])
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|DOMAIN=
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|RELATEDENTRY=[[2ju2|2JU2]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ju1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ju1 OCA], [http://www.ebi.ac.uk/pdbsum/2ju1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ju1 RCSB]</span>
}}
}}
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[[Category: transferase]]
[[Category: transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:45:03 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:01:39 2008''

Revision as of 01:01, 31 March 2008

Image:2ju1.jpg


PDB ID 2ju1

Drag the structure with the mouse to rotate
Gene: eryA (Saccharopolyspora erythraea)
Activity: Erythronolide synthase, with EC number 2.3.1.94
Related: 2JU2


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Solution structure of acyl carrier protein domain from module 2 of 6-deoxyerythronolide B synthase (DEBS)


Overview

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.

About this Structure

2JU1 is a Single protein structure of sequence from Saccharopolyspora erythraea. Full crystallographic 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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