1AY7

RIBONUCLEASE SA COMPLEX WITH BARSTAR

1AY7 の概要

• エントリーDOI: 10.2210/pdb1ay7/pdb
• 分子名称: GUANYL-SPECIFIC RIBONUCLEASE SA, BARSTAR (3 entities in total)
• 機能のキーワード: ribonuclease, inhibitor, streptomyces aureofaciens, complex (enzyme-inhibitor), complex (enzyme-inhibitor) complex, complex (enzyme/inhibitor)
• 由来する生物種: Streptomyces aureofaciens; 詳細
• 細胞内の位置: Secreted: P05798; Cytoplasm: P11540
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 20804.03

構造登録者

Sevcik, J.,Urbanikova, L.,Dauter, Z.,Wilson, K.S. (登録日: 1997-11-14, 公開日: 1999-03-02, 最終更新日: 2024-10-16)

主引用文献

Sevcik, J.,Urbanikova, L.,Dauter, Z.,Wilson, K.S.
Recognition of RNase Sa by the inhibitor barstar: structure of the complex at 1.7 A resolution.
Acta Crystallogr.,Sect.D, 54:954-963, 1998

PubMed Abstract: We report the 1.7 A resolution structure of RNase Sa complexed with the polypeptide inhibitor barstar. The crystals are in the hexagonal space group P65 with unit-cell dimensions a = b = 56.9, c = 135.8 A and the asymmetric unit contains one molecule of the complex. RNase Sa is an extracellular microbial ribonuclease produced by Streptomyces aureofaciens. Barstar is the natural inhibitor of barnase, the ribonuclease of Bacillus amyloliquefaciens. It inhibits RNase Sa and barnase in a similar manner by steric blocking of the active site. The structure of RNase Sa is very similar to that observed in crystals of the native enzyme and its complexes with nucleotides. Barstar retains the structure found in its complex with barnase. The accessible surface area of protein buried in the complex is about 300 A2 smaller and there are fewer hydrogen bonds in the enzyme-inhibitor interface in RNase Sa-barstar than in barnase-barstar, providing an explanation of the reduced binding affinity in the former. Previous studies of barstar complexes have used mutants of the inhibitor and this is the first structure which includes wild-type barstar.

PubMed: 9757110
DOI: 10.1107/S0907444998004429

実験手法

X-RAY DIFFRACTION (1.7 Å)