A left-handed beta-helix revealed by the crystal structure of a carbonic anhydrase from the archaeon Methanosarcina thermophila

被引:197
作者
Kisker, C
Schindelin, H
Alber, BE
Ferry, JG
Rees, DC
机构
[1] CALTECH,DIV CHEM & CHEM ENGN,PASADENA,CA 91125
[2] PENN STATE UNIV,DEPT BIOCHEM & MOLEC BIOL,UNIVERSITY PK,PA 16802
关键词
archaea; carbonic anhydrase; convergent evolution; left-handed; beta-helix;
D O I
10.1002/j.1460-2075.1996.tb00588.x
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
A carbonic anhydrase from the thermophilic archaeon Methanosarcina thermophila that exhibits no significant sequence similarity to known carbonic anhydrases has recently been characterized. Here we present the structure of this enzyme, which adopts a left-handed parallel beta-helix fold. This fold is of particular interest since it contains only left-handed crossover connections between the parallel beta-strands, which so far have been observed very infrequently. The active form of the enzyme is a trimer with three zinc-containing active sites, each located at the interface between two monomers. While the arrangement of active site groups differs between this enzyme and the carbonic anhydrases from higher vertebrates, there are structural similarities in the zinc coordination environment, suggestive of convergent evolution dictated by the chemical requirements for catalysis of the same reaction. Based on sequence similarities, the structure of this enzyme is the prototype of a new class of carbonic anhydrases with representatives in all three phylogenetic domains of life.
引用
收藏
页码:2323 / 2330
页数:8
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