1UGG
HUMAN CARBONIC ANHYDRASE II[HCAII] (E.C.4.2.1.1) MUTANT WITH ALA 65 REPLACED BY SER (A65S)-ORTHORHOMBIC FORM
Summary for 1UGG
Entry DOI | 10.2210/pdb1ugg/pdb |
Descriptor | CARBONIC ANHYDRASE II, ZINC ION (3 entities in total) |
Functional Keywords | lyase (oxo-acid), acetylation, zinc, polymorphism, disease mutation |
Biological source | Homo sapiens (human) |
Cellular location | Cytoplasm: P00918 |
Total number of polymer chains | 1 |
Total formula weight | 29152.19 |
Authors | Scolnick, L.R.,Christianson, D.W. (deposition date: 1996-07-24, release date: 1997-01-27, Last modification date: 2024-04-03) |
Primary citation | Scolnick, L.R.,Christianson, D.W. X-ray crystallographic studies of alanine-65 variants of carbonic anhydrase II reveal the structural basis of compromised proton transfer in catalysis. Biochemistry, 35:16429-16434, 1996 Cited by PubMed Abstract: The three-dimensional structures of A65F, A65L, A65H, A65T, A65S, and A65G human carbonic anhydrase II (CAII) variants have been solved by X-ray crystallographic methods to probe the importance of residue 65 and the structural implications of its evolutionary drift in the greater family of carbonic anhydrase isozymes. Structure-activity relationships in this series of CAII variants are correlated with those established for other carbonic anhydrase isozymes. We conclude that a bulky side chain at position 65 hinders the formation of an effective solvent bridge between zinc-bound water and H64 and thereby hinders solvent-mediated proton transfer between these two groups [Jackman, J. E., Merz, K. M., Jr., & Fierke, C. A. (1996) Biochemistry 35, 16421-16428]. Despite the introduction of a polar hydroxyl group at this position, smaller side chains such as serine or threonine substituted for A65 do not perturb the formation of a solvent bridge between H64 and zinc-bound solvent. Thus, the evolution of residue 65 size is one factor affecting the trajectory of catalytic proton transfer. PubMed: 8987974DOI: 10.1021/bi9617872 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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