1dmx
From Proteopedia
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|PDB= 1dmx |SIZE=350|CAPTION= <scene name='initialview01'>1dmx</scene>, resolution 2.45Å | |PDB= 1dmx |SIZE=350|CAPTION= <scene name='initialview01'>1dmx</scene>, resolution 2.45Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
| - | |ACTIVITY= [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] | + | |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> |
|GENE= MCA5C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | |GENE= MCA5C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dmx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dmx OCA], [http://www.ebi.ac.uk/pdbsum/1dmx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dmx RCSB]</span> | ||
}} | }} | ||
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[[Category: Boriack-Sjodin, P A.]] | [[Category: Boriack-Sjodin, P A.]] | ||
[[Category: Christianson, D W.]] | [[Category: Christianson, D W.]] | ||
| - | [[Category: ZN]] | ||
[[Category: proton transfer]] | [[Category: proton transfer]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:44:45 2008'' |
Revision as of 16:44, 30 March 2008
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| , resolution 2.45Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | MCA5C (Mus musculus) | ||||||
| Activity: | Carbonate dehydratase, with EC number 4.2.1.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
MURINE MITOCHONDRIAL CARBONIC ANYHDRASE V AT 2.45 ANGSTROMS RESOLUTION
Overview
The three-dimensional structure of murine mitochondrial carbonic anhydrase V has been determined and refined at 2.45-A resolution (crystallographic R factor = 0.187). Significant structural differences unique to the active site of carbonic anhydrase V are responsible for differences in the mechanism of catalytic proton transfer as compared with other carbonic anhydrase isozymes. In the prototypical isozyme, carbonic anhydrase II, catalytic proton transfer occurs via the shuttle group His-64; carbonic anhydrase V has Tyr-64, which is not an efficient proton shuttle due in part to the bulky adjacent side chain of Phe-65. Based on analysis of the structure of carbonic anhydrase V, we speculate that Tyr-131 may participate in proton transfer due to its proximity to zinc-bound solvent, its solvent accessibility, and its electrostatic environment in the protein structure. Finally, the design of isozyme-specific inhibitors is discussed in view of the complex between carbonic anhydrase V and acetazolamide, a transition-state analogue. Such inhibitors may be physiologically important in the regulation of blood glucose levels.
About this Structure
1DMX is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Structure determination of murine mitochondrial carbonic anhydrase V at 2.45-A resolution: implications for catalytic proton transfer and inhibitor design., Boriack-Sjodin PA, Heck RW, Laipis PJ, Silverman DN, Christianson DW, Proc Natl Acad Sci U S A. 1995 Nov 21;92(24):10949-53. PMID:7479916
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