5ca2: Difference between revisions

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[[Image:5ca2.gif|left|200px]]
{{Seed}}
[[Image:5ca2.png|left|200px]]


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{{STRUCTURE_5ca2|  PDB=5ca2  |  SCENE=  }}  
{{STRUCTURE_5ca2|  PDB=5ca2  |  SCENE=  }}  


'''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===




==Overview==
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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.
The line below this paragraph, {{ABSTRACT_PUBMED_1909891}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_1909891}}


==About this Structure==
==About this Structure==
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[[Category: Alexander, R S.]]
[[Category: Alexander, R S.]]
[[Category: Christianson, D W.]]
[[Category: Christianson, D W.]]
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