1dmx

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[[Image:1dmx.gif|left|200px]]<br /><applet load="1dmx" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1dmx.gif|left|200px]]
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caption="1dmx, resolution 2.45&Aring;" />
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'''MURINE MITOCHONDRIAL CARBONIC ANYHDRASE V AT 2.45 ANGSTROMS RESOLUTION'''<br />
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{{Structure
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|PDB= 1dmx |SIZE=350|CAPTION= <scene name='initialview01'>1dmx</scene>, resolution 2.45&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene>
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|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]
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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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'''MURINE MITOCHONDRIAL CARBONIC ANYHDRASE V AT 2.45 ANGSTROMS RESOLUTION'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1DMX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DMX OCA].
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1DMX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DMX OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7479916 7479916]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/7479916 7479916]
[[Category: Carbonate dehydratase]]
[[Category: Carbonate dehydratase]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: proton transfer]]
[[Category: proton transfer]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:18:18 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:41:03 2008''

Revision as of 08:41, 20 March 2008


PDB ID 1dmx

Drag the structure with the mouse to rotate
, resolution 2.45Å
Ligands:
Gene: MCA5C (Mus musculus)
Activity: Carbonate dehydratase, with EC number 4.2.1.1
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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