2KR5

Solution Structure of an Acyl Carrier Protein Domain from Fungal Type I Polyketide Synthase

2KR5 の概要

• エントリーDOI: 10.2210/pdb2kr5/pdb
• NMR情報: BMRB: 16624
• 分子名称: Aflatoxin biosynthesis polyketide synthase, 4'-PHOSPHOPANTETHEINE (2 entities in total)
• 機能のキーワード: acyl carrrier protein, holo, phosphopantetheine, aflatoxin biosynthesis, transport protein
• 由来する生物種: Aspergillus parasiticus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9787.94

構造登録者

Wattana-amorn, P.,Williams, C.,Ploskon, E.,Cox, R.J.,Simpson, T.J.,Crosby, J.,Crump, M.P. (登録日: 2009-12-03, 公開日: 2010-03-02, 最終更新日: 2024-05-22)

主引用文献

Wattana-amorn, P.,Williams, C.,Ploskon, E.,Cox, R.J.,Simpson, T.J.,Crosby, J.,Crump, M.P.
Solution structure of an acyl carrier protein domain from a fungal type I polyketide synthase.
Biochemistry, 49:2186-2193, 2010

PubMed Abstract: Acyl (peptidyl) carrier protein (ACP or PCP) is a crucial component involved in the transfer of thiol ester-bound intermediates during the biosynthesis of primary and secondary metabolites such as fatty acids, polyketides, and nonribosomal peptides. Although many carrier protein three-dimensional structures have been determined, to date there is no model available for a fungal type I polyketide synthase ACP. Here we report the solution structure of the norsolorinic acid synthase (NSAS) holo ACP domain that has been excised from the full-length multifunctional enzyme. NSAS ACP shows similarities in three-dimensional structure with other type I and type II ACPs, consisting of a four-helix bundle with helices I, II, and IV arranged in parallel. The N-terminus of helix III, however, is unusually hydrophobic, and Phe1768 and Leu1770 pack well with the core of the protein. The result is that unlike other carrier proteins, helix III lies almost perpendicular to the three major helices. Helix III is well-defined by numerous NMR-derived distance restraints and may be less flexible than counterparts in type II FAS and PKS ACPs. When the holo ACP is derivatized with a hexanoyl group, only minor changes are observed between the HSQC spectra of the two ACP species and no NOEs are observed for this hydrophobic acyl group. Along with the mammalian type I FAS, this further strengthens the view that type I ACPs do not show any significant affinity for hydrophobic (nonpolar) chain assembly intermediates attached via the 4'-phosphopantetheine prosthetic group.

PubMed: 20136099
DOI: 10.1021/bi902176v

実験手法

SOLUTION NMR