1ugf: Difference between revisions
New page: left|200px<br /> <applet load="1ugf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ugf, resolution 2.0Å" /> '''HUMAN CARBONIC ANHYD... |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1ugf. | [[Image:1ugf.jpg|left|200px]]<br /><applet load="1ugf" size="350" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="1ugf" size=" | |||
caption="1ugf, resolution 2.0Å" /> | caption="1ugf, resolution 2.0Å" /> | ||
'''HUMAN CARBONIC ANHYDRASE II [HCAII] (E.C.4.2.1.1) MUTANT WITH ALA 65 REPLACED BY THR (A65T)'''<br /> | '''HUMAN CARBONIC ANHYDRASE II [HCAII] (E.C.4.2.1.1) MUTANT WITH ALA 65 REPLACED BY THR (A65T)'''<br /> | ||
| Line 11: | Line 10: | ||
==About this Structure== | ==About this Structure== | ||
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 HG, ZN and AZI 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:// | 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]. | ||
==Reference== | ==Reference== | ||
| Line 29: | Line 28: | ||
[[Category: zinc]] | [[Category: zinc]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:02:03 2008'' | ||
Revision as of 18:02, 15 February 2008
|
HUMAN CARBONIC ANHYDRASE II [HCAII] (E.C.4.2.1.1) MUTANT WITH ALA 65 REPLACED BY THR (A65T)
OverviewOverview
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.
DiseaseDisease
Known disease associated with this structure: Osteopetrosis, autosomal recessive 3, with renal tubular acidosis OMIM:[611492]
About this StructureAbout this Structure
1UGF 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.
ReferenceReference
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 Fri Feb 15 17:02:03 2008