1CXU

1.42A RESOLUTION ASV INTEGRASE CORE DOMAIN FROM CITRATE

1CXU の概要

• エントリーDOI: 10.2210/pdb1cxu/pdb
• 関連するPDBエントリー: 1ASV 1CXQ 1CZ9 1CZB
• 分子名称: PROTEIN (AVIAN SARCOMA VIRUS INTEGRASE), CITRIC ACID, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: mixed beta-sheet surrounded by alpha-helices, transferase
• 由来する生物種: Avian sarcoma virus
• 細胞内の位置: Matrix protein p19: Virion (Potential). Capsid protein p27: Virion (Potential). Nucleocapsid protein p12: Virion (Potential): P03354
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18139.66

構造登録者

Lubkowski, J.,Dauter, Z.,Yang, F.,Alexandratos, J.,Wlodawer, A. (登録日: 1999-08-30, 公開日: 1999-09-08, 最終更新日: 2024-02-07)

主引用文献

Lubkowski, J.,Dauter, Z.,Yang, F.,Alexandratos, J.,Merkel, G.,Skalka, A.M.,Wlodawer, A.
Atomic resolution structures of the core domain of avian sarcoma virus integrase and its D64N mutant.
Biochemistry, 38:13512-13522, 1999

PubMed Abstract: Six crystal structures of the core domain of integrase (IN) from avian sarcoma virus (ASV) and its active-site derivative containing an Asp64 --> Asn substitution have been solved at atomic resolution ranging 1.02-1.42 A. The high-quality data provide new structural information about the active site of the enzyme and clarify previous inconsistencies in the description of this fragment. The very high resolution of the data and excellent quality of the refined models explain the dynamic properties of IN and the multiple conformations of its disordered residues. They also allow an accurate description of the solvent structure and help to locate other molecules bound to the enzyme. A detailed analysis of the flexible active-site region, in particular the loop formed by residues 144-154, suggests conformational changes which may be associated with substrate binding and enzymatic activity. The pH-dependent conformational changes of the active-site loop correlates with the pH vs activity profile observed for ASV IN.

PubMed: 10521258
DOI: 10.1021/bi991362q

実験手法

X-RAY DIFFRACTION (1.42 Å)