The Active Site Structure of Thalassiosira weissflogii Carbonic Anhydrase 1

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 α-carbonic anhydrase enzymes. The zinc has three histidine ligands and a single water at 1.98 Å. This is quite di...

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Bibliographic Details
Published in:	Biochemistry (Easton) Vol. 39; no. 40; pp. 12128 - 12130
Main Authors:	Cox, Elizabeth H, McLendon, George L, Morel, François M. M, Lane, Todd W, Prince, Roger C, Pickering, Ingrid J, George, Graham N
Format:	Journal Article
Language:	English
Published:	United States American Chemical Society 10-10-2000
Subjects:	Animals Binding Sites Carbonic Anhydrases - chemistry Carbonic Anhydrases - metabolism Cattle Diatoms - enzymology Fourier Analysis Scattering, Radiation Spectrum Analysis Spinacia oleracea - enzymology Thalassiosira weissflogii X-Rays Zinc - chemistry Zinc - metabolism
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Summary:	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 α-carbonic anhydrase enzymes. The zinc has three histidine ligands and a single water at 1.98 Å. This is quite different from the β-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.
Bibliography:	E.H.C. was supported by a Camille and Henry Dreyfus Postdoctoral Fellowship in Environmental Sciences. Research at Princeton University is supported through funding from the Center for Environmental Bioinorganic Chemistry (CEBIC), which is supported by the NSF and DOE. SSRL is funded by the Department of Energy, Office of Basic Energy Sciences, under Contract DE-AC03-76SF00515. The SSRL Structural Molecular Biology Program is supported by the National Institutes of Health, National Center for Research Resources, Biomedical Technology Program, and by the Department of Energy, Office of Biological and Environmental Research. istex:450573FD60B567DD527FC06E92906DD391DC9EDF ark:/67375/TPS-DHW2FKWJ-X ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2
ISSN:	0006-2960 1520-4995
DOI:	10.1021/bi001416s