1ugc
From Proteopedia
(New page: 200px<br /> <applet load="1ugc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ugc, resolution 2.0Å" /> '''HUMAN CARBONIC ANHYD...) |
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caption="1ugc, resolution 2.0Å" /> | caption="1ugc, resolution 2.0Å" /> | ||
'''HUMAN CARBONIC ANHYDRASE II [HCAII] (E.C.4.2.1.1) MUTANT WITH ALA 65 REPLACED BY HIS (A65H)'''<br /> | '''HUMAN CARBONIC ANHYDRASE II [HCAII] (E.C.4.2.1.1) MUTANT WITH ALA 65 REPLACED BY HIS (A65H)'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1UGC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with HG and ZN as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Carbonate_dehydratase Carbonate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.1 4.2.1.1] Full crystallographic information is available from [http:// | + | 1UGC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=HG:'>HG</scene> and <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Carbonate_dehydratase Carbonate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.1 4.2.1.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UGC OCA]. |
==Reference== | ==Reference== | ||
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[[Category: zinc]] | [[Category: zinc]] | ||
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Revision as of 15:01, 15 February 2008
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HUMAN CARBONIC ANHYDRASE II [HCAII] (E.C.4.2.1.1) MUTANT WITH ALA 65 REPLACED BY HIS (A65H)
Contents |
Overview
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.
Disease
Known disease associated with this structure: Osteopetrosis, autosomal recessive 3, with renal tubular acidosis OMIM:[611492]
About this Structure
1UGC 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
X-ray crystallographic studies of alanine-65 variants of carbonic anhydrase II reveal the structural basis of compromised proton transfer in catalysis., Scolnick LR, Christianson DW, Biochemistry. 1996 Dec 24;35(51):16429-34. PMID:8987974
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