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 ZN and ACY 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 Mon Nov 12 16:19:37 2007
Categories: Carbonate dehydratase | Homo sapiens | Single protein | Briand, C. | Hakansson, K. | Liljas, A. | Xue, Y. | Zaitsev, V. | ACY | ZN | Lyase(oxo-acid)
