X-ray analysis of metal-substituted human carbonic anhydrase II derivatives.

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Hakansson K, Wehnert A, Liljas A

X-ray analysis of metal-substituted human carbonic anhydrase II derivatives.

Acta Crystallogr D Biol Crystallogr. 1994 Jan 1;50(Pt 1):93-100.

PubMed ID
15299481 [ View in PubMed
]
Abstract

Metal-substituted crystals of human carbonic anhydrase II belonging to space group P2(1) with cell dimensions a = 42.7, b = 41.7, c = 73.0 A and beta = 104.6 degrees were analyzed crystallographically. The resolution limit ranged from 1.82 to 1.92 A with high completeness (86.2-90.7%). Cobalt(II)-substituted carbonic anhydrase has a tetrahedral coordination around the metal both at pH 6 and pH 7.8, similar to the native zinc enzyme. In contrast, the catalytically inactive copper(II), nickel(II) and manganese(II) derivatives showed increased coordination number around the metal ion. Whereas the copper is best described as penta-coordinated, the nickel and manganese are best described as hexa-coordinated. The results are briefly compared with spectroscopic observations and our current view on carbonic anhydrase catalysis.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Carbonic anhydrase 2P00918Details