1B2U

STRUCTURAL RESPONSE TO MUTATION AT A PROTEIN-PROTEIN INTERFACE

1B2U の概要

• エントリーDOI: 10.2210/pdb1b2u/pdb
• 分子名称: PROTEIN (BARNASE), PROTEIN (BARSTAR) (3 entities in total)
• 機能のキーワード: rnase-inhibitor complex, interfacial double mutant, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• 由来する生物種: Bacillus amyloliquefaciens; 詳細
• 細胞内の位置: Secreted: P00648; Cytoplasm: P11540
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 67948.04

構造登録者

Vaughan, C.K.,Buckle, A.M.,Fersht, A.R. (登録日: 1998-12-01, 公開日: 1998-12-09, 最終更新日: 2023-08-09)

主引用文献

Vaughan, C.K.,Buckle, A.M.,Fersht, A.R.
Structural response to mutation at a protein-protein interface.
J.Mol.Biol., 286:1487-1506, 1999

PubMed Abstract: We have crystallised three mutants of the barnase-barstar complex in which interactions across the interface have been deleted by simultaneous mutation of both residues involved in the interaction. Each mutant deletes a different type of interaction at the interface: the first complex bnHis102-->Ala-bsTyr29-->Phe (bn, barnase; bs, barstar), deletes a van der Waals packing interaction; the second complex, bnLys27-->Ala-bsThr42-->Ala, deletes a hydrogen bond; the third, bnLys27-->Ala-bsAsp35-->Ala, deletes a long-range charge-charge interaction. The contribution of each of these side-chains to the stability of the complex is known; the coupling energy between the deleted side-chains is also known. Despite each of the double mutants being significantly destabilised compared with the wild-type, the effects of mutation are local. Only small movements in the main-chain surrounding the sites of mutation and some larger movements of neighbouring side-chains are observed in the mutant complexes. The exact response to mutation is context-dependent and for the same mutant can vary depending upon the environment within the crystal. In some double mutant complexes, interfacial pockets, which are accessible to bulk solvent are formed, whereas interfacial cavities which are isolated from bulk solvent, are formed in others. In all double mutants, water molecules fill the created pockets and cavities. These water molecules mimic the deleted side-chains by occupying positions close to the non-carbon atoms of truncated side-chains and re-making many hydrogen bonds made by the truncated side-chains in the wild-type. It remains extremely difficult, however, to correlate energetic and structural responses to mutation because of unknown changes in entropy and entropy-enthalpy compensation.

PubMed: 10064711
DOI: 10.1006/jmbi.1998.2559

実験手法

X-RAY DIFFRACTION (2.1 Å)