1ugd

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[[Image:1ugd.jpg|left|200px]]
[[Image:1ugd.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1ugd |SIZE=350|CAPTION= <scene name='initialview01'>1ugd</scene>, resolution 2.0&Aring;
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The line below this paragraph, containing "STRUCTURE_1ugd", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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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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|DOMAIN=
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{{STRUCTURE_1ugd| PDB=1ugd | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ugd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ugd OCA], [http://www.ebi.ac.uk/pdbsum/1ugd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ugd RCSB]</span>
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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 SER (A65S)'''
'''HUMAN CARBONIC ANHYDRASE II[HCAII] (E.C.4.2.1.1) MUTANT WITH ALA 65 REPLACED BY SER (A65S)'''
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[[Category: Christianson, D W.]]
[[Category: Christianson, D W.]]
[[Category: Scolnick, L R.]]
[[Category: Scolnick, L R.]]
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[[Category: acetylation]]
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[[Category: Acetylation]]
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[[Category: disease mutation]]
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[[Category: Disease mutation]]
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[[Category: lyase (oxo-acid)]]
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[[Category: Polymorphism]]
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[[Category: polymorphism]]
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[[Category: Zinc]]
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[[Category: zinc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:11:32 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:09:53 2008''
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Revision as of 08:11, 3 May 2008

Image:1ugd.jpg

Template:STRUCTURE 1ugd

HUMAN CARBONIC ANHYDRASE II[HCAII] (E.C.4.2.1.1) MUTANT WITH ALA 65 REPLACED BY SER (A65S)


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.

About this Structure

1UGD 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 Page seeded by OCA on Sat May 3 11:11:32 2008

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