2JU2

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

2JU2 の概要

• エントリーDOI: 10.2210/pdb2ju2/pdb
• 関連するPDBエントリー: 2ju1
• 分子名称: Erythronolide synthase (1 entity in total)
• 機能のキーワード: carrier protein domain, modular polyketide synthase, alpha-helical bundle, acyltransferase, antibiotic biosynthesis, multifunctional enzyme, nadp, phosphopantetheine, transferase
• 由来する生物種: Saccharopolyspora erythraea
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10160.62

構造登録者

Alekseyev, V.Y.,Liu, C.W.,Puglisi, J.D.,Khosla, C. (登録日: 2007-08-12, 公開日: 2007-10-02, 最終更新日: 2024-05-29)

主引用文献

Alekseyev, V.Y.,Liu, C.W.,Cane, D.E.,Puglisi, J.D.,Khosla, C.
Solution structure and proposed domain domain recognition interface of an acyl carrier protein domain from a modular polyketide synthase.
Protein Sci., 16:2093-2107, 2007

PubMed Abstract: 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.

PubMed: 17893358
DOI: 10.1110/ps.073011407

実験手法

SOLUTION NMR