1rj5: Difference between revisions

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[[Image:1rj5.jpg|left|200px]]<br /><applet load="1rj5" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1rj5.jpg|left|200px]]
caption="1rj5, resolution 2.81&Aring;" />
 
'''Crystal Structure of the Extracellular Domain of Murine Carbonic Anhydrase XIV'''<br />
{{Structure
|PDB= 1rj5 |SIZE=350|CAPTION= <scene name='initialview01'>1rj5</scene>, resolution 2.81&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> and <scene name='pdbligand=ACY:ACETIC ACID'>ACY</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]
|GENE= CA14, CAR14, CATM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
}}
 
'''Crystal Structure of the Extracellular Domain of Murine Carbonic Anhydrase XIV'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1RJ5 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>, <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=ACY:'>ACY</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1RJ5 OCA].  
1RJ5 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=1RJ5 OCA].  


==Reference==
==Reference==
Expression, assay, and structure of the extracellular domain of murine carbonic anhydrase XIV: implications for selective inhibition of membrane-associated isozymes., Whittington DA, Grubb JH, Waheed A, Shah GN, Sly WS, Christianson DW, J Biol Chem. 2004 Feb 20;279(8):7223-8. Epub 2003 Dec 3. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14660577 14660577]
Expression, assay, and structure of the extracellular domain of murine carbonic anhydrase XIV: implications for selective inhibition of membrane-associated isozymes., Whittington DA, Grubb JH, Waheed A, Shah GN, Sly WS, Christianson DW, J Biol Chem. 2004 Feb 20;279(8):7223-8. Epub 2003 Dec 3. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14660577 14660577]
[[Category: Carbonate dehydratase]]
[[Category: Carbonate dehydratase]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: zinc enzyme]]
[[Category: zinc enzyme]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:51:26 2008''
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Revision as of 14:52, 20 March 2008

File:1rj5.jpg


PDB ID 1rj5

Drag the structure with the mouse to rotate
, resolution 2.81Å
Ligands: , and
Gene: CA14, CAR14, CATM (Mus musculus)
Activity: Carbonate dehydratase, with EC number 4.2.1.1
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of the Extracellular Domain of Murine Carbonic Anhydrase XIV


OverviewOverview

Carbonic anhydrase (CA) XIV is the most recently identified mammalian carbonic anhydrase isozyme, and its presence has been demonstrated in a number of tissues. Full-length CA XIV is a transmembrane protein composed of an extracellular catalytic domain, a single transmembrane helix, and a short intracellular polypeptide segment. The amino acid sequence identity of human CA XIV relative to the other membrane-associated isozymes (CA IV, CA IX, and CA XII) is 34-46%. We report here the expression and purification of both the full-length enzyme and a truncated, secretory form of murine CA XIV. Both forms of this isozyme are highly active, and both show an abrogation of activity in the presence of 0.2% SDS, in contrast to the behavior of murine CA IV. We also report the crystal structure of the extracellular domain of murine CA XIV at 2.8 A resolution and of an enzyme-acetazolamide complex at 2.9 A resolution. The structure shows a monomeric glycoprotein with a topology similar to that of other mammalian CA isozymes. Based on the x-ray crystallographic results, we compare and contrast known structures of membrane-associated CA isozymes to rationalize the structural elements responsible for the SDS resistance of CA IV and to discuss prospects for the design of selective inhibitors of membrane-associated CA isozymes.

About this StructureAbout this Structure

1RJ5 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

Expression, assay, and structure of the extracellular domain of murine carbonic anhydrase XIV: implications for selective inhibition of membrane-associated isozymes., Whittington DA, Grubb JH, Waheed A, Shah GN, Sly WS, Christianson DW, J Biol Chem. 2004 Feb 20;279(8):7223-8. Epub 2003 Dec 3. PMID:14660577

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