REFINED STRUCTURE OF BOVINE CARBONIC ANHYDRASE-III AT 2.0 ANGSTROM RESOLUTION

被引:108
作者
ERIKSSON, AE
LILJAS, A
机构
[1] UNIV LUND,CTR CHEM,DEPT MOLEC BIOPHYS,BOX 124,S-22100 LUND,SWEDEN
[2] UPPSALA UNIV,CTR BIOMED,DEPT MOLEC BIOL,S-75124 UPPSALA,SWEDEN
来源
PROTEINS-STRUCTURE FUNCTION AND GENETICS | 1993年 / 16卷 / 01期
关键词
CRYSTALLOGRAPHY; MOLECULAR REPLACEMENT; REFINEMENT; STRUCTURE; MUSCLE; CARBONIC ANHYDRASE;
D O I
10.1002/prot.340160104
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The three-dimensional structure of bovine carbonic anhydrase III (BCA III) from red skeletal muscle cells has been determined by molecular replacement methods. The structure has been refined at 2.0 angstrom resolution by both constrained and restrained structure-factor least squares refinement. The current crystallographic R-value is 19.2% and 121 solvent molecules have so far been found associated with the protein. The structure is highly similar to the refined structure of human carbonic anhydrase II. Some differences in amino acid sequence and structure between the two isoenzymes are discussed. In BCA III, Lys 64 and Arg 91 (His 64 and Ile 91 in HCA II) are both pointing out from the active site cavity forming salt bridges with Glu 4 and Asp 72 (His 4 and Asp 72 in HCA II), respectively. However, Arg 67 and Phe 198 (Asn 67 and Leu 198 in HCA II) are oriented towards the zinc ion and significantly reduce the volume of the active site cavity. Phe 198 particularly reduces the size of the substrate binding region at the ''deep water'' position at the bottom of the cavity and we suggest that this is one of the major reasons for the differences in catalytic properties of isoenzyme III as compared to isozyme II.
引用
收藏
页码:29 / 42
页数:14
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