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New page: left|200px<br /><applet load="1rj6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rj6, resolution 2.90Å" /> '''Crystal Structure of...
 
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[[Image:1rj6.jpg|left|200px]]<br /><applet load="1rj6" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1rj6, resolution 2.90&Aring;" />
'''Crystal Structure of the Extracellular Domain of Murine Carbonic Anhydrase XIV in Complex with Acetazolamide'''<br />


==Overview==
==Crystal Structure of the Extracellular Domain of Murine Carbonic Anhydrase XIV in Complex with Acetazolamide==
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.
<StructureSection load='1rj6' size='340' side='right'caption='[[1rj6]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1rj6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RJ6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RJ6 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AZM:5-ACETAMIDO-1,3,4-THIADIAZOLE-2-SULFONAMIDE'>AZM</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1rj6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rj6 OCA], [https://pdbe.org/1rj6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rj6 RCSB], [https://www.ebi.ac.uk/pdbsum/1rj6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rj6 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CAH14_MOUSE CAH14_MOUSE] Reversible hydration of carbon dioxide.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rj/1rj6_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1rj6 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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 Structure==
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<ref>PMID:14660577</ref>
1RJ6 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 ZN and AZM 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RJ6 OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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]
</div>
[[Category: Carbonate dehydratase]]
<div class="pdbe-citations 1rj6" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Carbonic anhydrase 3D structures|Carbonic anhydrase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Christianson DW]]
[[Category: Christianson, D.W.]]
[[Category: Grubb JH]]
[[Category: Grubb, J.H.]]
[[Category: Shah GN]]
[[Category: Shah, G.N.]]
[[Category: Sly WS]]
[[Category: Sly, W.S.]]
[[Category: Waheed A]]
[[Category: Waheed, A.]]
[[Category: Whittington DA]]
[[Category: Whittington, D.A.]]
[[Category: AZM]]
[[Category: ZN]]
[[Category: alpha-helix]]
[[Category: beta-sheet]]
[[Category: zinc enzyme]]
 
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