4PK0

CRYSTAL STRUCTURE OF T4 LYSOZYME-PEPTIDE IN COMPLEX WITH TEICOPLANIN-A2-2

4PK0 の概要

• エントリーDOI: 10.2210/pdb4pk0/pdb
• 関連するPDBエントリー: 4PJZ
• 関連するBIRD辞書のPRD_ID: PRD_002089
• 分子名称: TEICOPLANIN-A2-2, GLYCEROL, Lysozyme, ... (11 entities in total)
• 機能のキーワード: site-selective catalyst, carrier protein approach, glycopeptide antibiotic, hydrolase-antibiotic complex, hydrolase/antibiotic
• 由来する生物種: Enterobacteria phage T4; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 21541.46

構造登録者

Han, S.,Le, B.V.,Hajare, H.,Baxter, R.H.G.,Miller, S.J. (登録日: 2014-05-13, 公開日: 2014-09-10, 最終更新日: 2023-12-27)

主引用文献

Han, S.,Le, B.V.,Hajare, H.S.,Baxter, R.H.,Miller, S.J.
X-ray Crystal Structure of Teicoplanin A2-2 Bound to a Catalytic Peptide Sequence via the Carrier Protein Strategy.
J.Org.Chem., 79:8550-8556, 2014

PubMed Abstract: We report the X-ray crystal structure of a site-selective peptide catalyst moiety and teicoplanin A2-2 complex. The expressed protein ligation technique was used to couple T4 lysozyme (T4L) and a synthetic peptide catalyst responsible for the selective phosphorylation of the N-acetylglucosamine sugar in a teicoplanin A2-2 derivative. The T4L-Pmh-dPro-Aib-dAla-dAla construct was crystallized in the presence of teicoplanin A2-2. The resulting 2.3 Å resolution protein-peptide-teicoplanin complex crystal structure revealed that the nucleophilic nitrogen of N-methylimidazole in the Pmh residue is in closer proximity (7.6 Å) to the N-acetylglucosamine than the two other sugar rings present in teicoplanin (9.3 and 20.3 Å, respectively). This molecular arrangement is consistent with the observed selectivity afforded by the peptide-based catalyst when it is applied to a site-selective phosphorylation reaction involving a teicoplanin A2-2 derivative.

PubMed: 25147913
DOI: 10.1021/jo501625f

実験手法

X-RAY DIFFRACTION (2.3 Å)