5ca2

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[[Image:5ca2.gif|left|200px]]
[[Image:5ca2.gif|left|200px]]
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{{Structure
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|PDB= 5ca2 |SIZE=350|CAPTION= <scene name='initialview01'>5ca2</scene>, resolution 2.1&Aring;
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The line below this paragraph, containing "STRUCTURE_5ca2", creates the "Structure Box" on the page.
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|LIGAND= <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <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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{{STRUCTURE_5ca2| PDB=5ca2 | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ca2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ca2 OCA], [http://www.ebi.ac.uk/pdbsum/5ca2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=5ca2 RCSB]</span>
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'''CONFORMATIONAL MOBILITY OF HIS-64 IN THE THR-200 (RIGHT ARROW) SER MUTANT OF HUMAN CARBONIC ANHYDRASE II'''
'''CONFORMATIONAL MOBILITY OF HIS-64 IN THE THR-200 (RIGHT ARROW) SER MUTANT OF HUMAN CARBONIC ANHYDRASE II'''
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[[Category: Alexander, R S.]]
[[Category: Alexander, R S.]]
[[Category: Christianson, D W.]]
[[Category: Christianson, D W.]]
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[[Category: lyase(oxo-acid)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:32:21 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:40:55 2008''
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Revision as of 19:32, 4 May 2008

Image:5ca2.gif

Template:STRUCTURE 5ca2

CONFORMATIONAL MOBILITY OF HIS-64 IN THE THR-200 (RIGHT ARROW) SER MUTANT OF HUMAN CARBONIC ANHYDRASE II


Overview

The three-dimensional structure of the Thr-200----Ser (T200S) mutant of human carbonic anhydrase II (CAII) has been determined by X-ray crystallographic methods at 2.1-A resolution. This particular mutant of CAII exhibits CO2 hydrase activity that is comparable to that of the wild-type enzyme with a 2-fold stabilization of the E.HCO3- complex and esterase activity that is 4-fold greater than that of the wild-type enzyme. The structure of the mutant enzyme reveals no significant local changes accompanying the conservative T200S substitution, but an important nonlocal structural change is evident: the side chain of catalytic residue His-64 rotates away from the active site by 105 degrees about chi 1 and apparently displaces a water molecule. The displaced water molecule is present in the wild-type enzyme; however, the electron density into which this water is built is interpretable as an alternate conformation of His-64 with 10-20% occupancy. The rate constants for proton transfer from the zinc-water ligand to His-64 and from His-64 to bulk solvent are maintained in the T200S variant; therefore, if His-64 is conformationally mobile about chi 1 and/or chi 2 during catalysis, compensatory changes in solvent configuration must sustain efficient proton transfer.

About this Structure

5CA2 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Conformational mobility of His-64 in the Thr-200----Ser mutant of human carbonic anhydrase II., Krebs JF, Fierke CA, Alexander RS, Christianson DW, Biochemistry. 1991 Sep 24;30(38):9153-60. PMID:1909891 Page seeded by OCA on Sun May 4 22:32:21 2008

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