1cay
From Proteopedia
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WILD-TYPE AND E106Q MUTANT CARBONIC ANHYDRASE COMPLEXED WITH ACETATE
Contents |
Overview
The molecular structures of the acetate complexes of wild-type human, carbonic anhydrase II (HCAII) and of E106Q mutant human carbonic anhydrase, II were solved with high completeness (89-91%) to 2.1 and 1.9 A, resolution, respectively. Both wild-type and mutant enzyme crystallize in, space group P2(1) with cell dimensions a = 42.7, b = 41.7, c = 73.0 A and, beta = 104.6 degrees. The altered active-site hydrogen-bond network caused, by the mutation results in a different binding of the inhibitor in the two, complexes. In the mutant, but not in the wild-type complex, a carboxylate, O atom is within hydrogen-bond distance of Thr199 Ogamma1. In the, wild-type enzyme ligand hydrogen bonding to this atom is normally only, found for hydrogen-bond donors. The importance of this discrimination on, catalysis by the enzyme is discussed briefly.
Disease
Known disease associated with this structure: Osteopetrosis, autosomal recessive 3, with renal tubular acidosis OMIM:[611492]
About this Structure
1CAY is a Single protein structure of sequence from Homo sapiens with and as ligands. Active as Carbonate dehydratase, with EC number 4.2.1.1 Full crystallographic information is available from OCA.
Reference
Wild-type and E106Q mutant carbonic anhydrase complexed with acetate., Hakansson K, Briand C, Zaitsev V, Xue Y, Liljas A, Acta Crystallogr D Biol Crystallogr. 1994 Jan 1;50(Pt 1):101-4. PMID:15299482
Page seeded by OCA on Fri Feb 15 15:34:50 2008
Categories: Carbonate dehydratase | Homo sapiens | Single protein | Briand, C. | Hakansson, K. | Liljas, A. | Xue, Y. | Zaitsev, V. | ACY | ZN | Lyase(oxo-acid)
