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| - | [[Image:2hfw.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2hfw| PDB=2hfw | SCENE= }} | | {{STRUCTURE_2hfw| PDB=2hfw | SCENE= }} |
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| - | '''Structural and kinetic analysis of proton shuttle residues in the active site of human carbonic anhydrase III'''
| + | ===Structural and kinetic analysis of proton shuttle residues in the active site of human carbonic anhydrase III=== |
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| - | ==Overview==
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| - | We report the X-ray crystal structures and rate constants for proton transfer in site-specific mutants of human carbonic anhydrase III (HCA III) that place a histidine residue in the active-site cavity: K64H, R67H, and K64H-R67N HCA III. Prior evidence from the exchange of 18O between CO2 and water measured by mass spectrometry shows each mutant to have enhanced proton transfer in catalysis compared with wild-type HCA III. However, His64 in K64H and K64H-R67N HCA III have at most a capacity for proton transfer that is only 13% that of His64 in HCA II. This reduced rate in mutants of HCA III is associated with a constrained side-chain conformation of His64, which is oriented outward, away from the active-site zinc in the crystal structures. This conformation appears stabilized by a prominent pi stacking interaction of the imidazole ring of His64 with the indole ring of Trp5 in mutants of HCA III. This single orientation of His64 in K64H HCA III predominates also in a double mutant K64H-R67N HCA III, indicating that the positive charge of Arg67 does not influence the observed conformation of His64 in the crystal structure. Hence, the structures and catalytic activity of these mutants of HCA III containing His64 account only in small part for the lower activity of this isozyme compared with HCA II. His67 in R67H HCA III was also shown to be a proton shuttle residue, having a capacity for proton transfer that was approximately four times that of His64 in K64H HCA III. This is most likely due to its proximity and orientation inward towards the zinc-bound solvent. These results emphasize the significance of side chain orientation and range of available conformational states as characteristics of an efficient proton shuttle in carbonic anhydrase.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_17427958}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 17427958 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_17427958}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Proton shuttle]] | | [[Category: Proton shuttle]] |
| | [[Category: Proton transfer]] | | [[Category: Proton transfer]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:14:35 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 08:37:09 2008'' |
Revision as of 05:37, 29 July 2008
Template:STRUCTURE 2hfw
Structural and kinetic analysis of proton shuttle residues in the active site of human carbonic anhydrase III
Template:ABSTRACT PUBMED 17427958
About this Structure
2HFW is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural and kinetic analysis of proton shuttle residues in the active site of human carbonic anhydrase III., Elder I, Fisher Z, Laipis PJ, Tu C, McKenna R, Silverman DN, Proteins. 2007 Jul 1;68(1):337-43. PMID:17427958
Page seeded by OCA on Tue Jul 29 08:37:09 2008
