The active site structure of Thalassiosira weissflogii carbonic anhydrase 1

被引:102
作者
Cox, EH
McLendon, GL
Morel, FMM
Lane, TW
Prince, RC
Pickering, IJ
George, GN
机构
[1] Stanford Univ, Stanford Synchrotron Radiat Lab, SLAC, Stanford, CA 94309 USA
[2] Princeton Univ, Dept Chem, Ctr Environm Bioinorgan Chem, Princeton, NJ 08544 USA
[3] Princeton Univ, Dept Geosci, Princeton, NJ 08544 USA
[4] ExxonMobil Res & Engn Co, Annandale, NJ 08801 USA
关键词
D O I
10.1021/bi001416s
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
X-ray absorption spectroscopy at the Zn K-edge indicates that the active site of the marine diatom Thalassiosira weissflogii carbonic anhydrase is strikingly similar to that of mammalian alpha-carbonic anhydrase enzymes. The zinc has three histidine ligands and a single water at 1.98 Angstrom. This is quite different from the beta-carbonic anhydrases of higher plants in which zinc is coordinated by two cysteine thiolates, one histidine, and a water molecule. The diatom carbonic anhydrase shows no significant sequence similarity with other carbonic anhydrases and may represent an example of convergent evolution at the molecular level.
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页码:12128 / 12130
页数:3
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