Kannan K K, Notstrand B, Fridborg K, Lövgren S, Ohlsson A, Petef M
Proc Natl Acad Sci U S A. 1975 Jan;72(1):51-5. doi: 10.1073/pnas.72.1.51.
The three-dimensional structure of carbonic anhydrase B (EC 4,2,1,1; carbonate hydro-lyase) from human erythrocytes has been determined to high resolution. Parallel and antiparallel pleated sheet makes up the predominant secondary structure of the enzyme. The tertiary structure is unique for its folding and is very similar to the structure is unique for its folding and is very similar to the structure of the isoenzyme, human erythrocyte carbonic anhydrase C. The essential metal ion, zinc, is firmly bound to the enzyme through three histidyl ligands and located at the bottom of a 12-A deep conical cavity. The zinc ligands are involved in a number of hydrogen bond formations with residues in the immediate vicinity of the active site cavity. Some of the similarities and differences in the sidechain orientation and active site topography of the two isoenzymes are also discussed.
已将人红细胞碳酸酐酶B(EC 4,2,1,1;碳酸水解酶)的三维结构测定到高分辨率。平行和反平行褶皱片构成了该酶的主要二级结构。其三级结构因其折叠方式而独特,并且与同工酶人红细胞碳酸酐酶C的结构非常相似。必需金属离子锌通过三个组氨酸配体与该酶牢固结合,并位于一个12埃深的圆锥形腔底部。锌配体与活性位点腔紧邻区域的残基形成了许多氢键。还讨论了这两种同工酶在侧链取向和活性位点拓扑结构方面的一些异同。