1ugf

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[[Image:1ugf.jpg|left|200px]]<br /><applet load="1ugf" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ugf.jpg|left|200px]]
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caption="1ugf, resolution 2.0&Aring;" />
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'''HUMAN CARBONIC ANHYDRASE II [HCAII] (E.C.4.2.1.1) MUTANT WITH ALA 65 REPLACED BY THR (A65T)'''<br />
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{{Structure
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|PDB= 1ugf |SIZE=350|CAPTION= <scene name='initialview01'>1ugf</scene>, resolution 2.0&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=AZI:AZIDE ION'>AZI</scene>
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|ACTIVITY= [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]
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|GENE= CAII ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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}}
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'''HUMAN CARBONIC ANHYDRASE II [HCAII] (E.C.4.2.1.1) MUTANT WITH ALA 65 REPLACED BY THR (A65T)'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1UGF 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>, <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=AZI:'>AZI</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=1UGF OCA].
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1UGF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UGF OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8987974 8987974]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/8987974 8987974]
[[Category: Carbonate dehydratase]]
[[Category: Carbonate dehydratase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: zinc]]
[[Category: zinc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:24:11 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:31:38 2008''

Revision as of 12:31, 20 March 2008

Image:1ugf.jpg


PDB ID 1ugf

Drag the structure with the mouse to rotate
, resolution 2.0Å
Ligands: , and
Gene: CAII (Homo sapiens)
Activity: Carbonate dehydratase, with EC number 4.2.1.1
Coordinates: save as pdb, mmCIF, xml



HUMAN CARBONIC ANHYDRASE II [HCAII] (E.C.4.2.1.1) MUTANT WITH ALA 65 REPLACED BY THR (A65T)


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

1UGF is a Single protein structure of sequence from Homo sapiens. 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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