1dmx

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[[Image:1dmx.gif|left|200px]]
[[Image:1dmx.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1dmx |SIZE=350|CAPTION= <scene name='initialview01'>1dmx</scene>, resolution 2.45&Aring;
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The line below this paragraph, containing "STRUCTURE_1dmx", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <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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or leave the SCENE parameter empty for the default display.
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|GENE= MCA5C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
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-->
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|DOMAIN=
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{{STRUCTURE_1dmx| PDB=1dmx | SCENE= }}
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|RELATEDENTRY=
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|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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}}
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'''MURINE MITOCHONDRIAL CARBONIC ANYHDRASE V AT 2.45 ANGSTROMS RESOLUTION'''
'''MURINE MITOCHONDRIAL CARBONIC ANYHDRASE V AT 2.45 ANGSTROMS RESOLUTION'''
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[[Category: Boriack-Sjodin, P A.]]
[[Category: Boriack-Sjodin, P A.]]
[[Category: Christianson, D W.]]
[[Category: Christianson, D W.]]
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[[Category: proton transfer]]
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[[Category: Proton transfer]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:02:18 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:44:45 2008''
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Revision as of 11:02, 2 May 2008

Image:1dmx.gif

Template:STRUCTURE 1dmx

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 Page seeded by OCA on Fri May 2 14:02:18 2008

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