1rj5: Difference between revisions

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-[[Image:1rj5.png|left|200px]]
-{{STRUCTURE_1rj5|  PDB=1rj5  |  SCENE=  }}
+==Crystal Structure of the Extracellular Domain of Murine Carbonic Anhydrase XIV==
+<StructureSection load='1rj5' size='340' side='right'caption='[[1rj5]], [[Resolution|resolution]] 2.81&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1rj5]] 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=1RJ5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RJ5 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]] 2.81&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=1rj5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rj5 OCA], [https://pdbe.org/1rj5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rj5 RCSB], [https://www.ebi.ac.uk/pdbsum/1rj5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rj5 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/1rj5_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=1rj5 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.
-===Crystal Structure of the Extracellular Domain of Murine Carbonic Anhydrase XIV===
+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>
-{{ABSTRACT_PUBMED_14660577}}
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-==About this Structure==
+<div class="pdbe-citations 1rj5" style="background-color:#fffaf0;"></div>
-[[1rj5]] is a 2 chain structure of [[Carbonic anhydrase]] with 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].
 ==See Also==
-*[[Carbonic anhydrase|Carbonic anhydrase]]
+*[[Carbonic anhydrase 3D structures|Carbonic anhydrase 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:014660577</ref><references group="xtra"/>
+__TOC__
-[[Category: Carbonate dehydratase]]
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Mus musculus]]
-[[Category: Christianson, D W.]]
+[[Category: Christianson DW]]
-[[Category: Grubb, J H.]]
+[[Category: Grubb JH]]
-[[Category: Shah, G N.]]
+[[Category: Shah GN]]
-[[Category: Sly, W S.]]
+[[Category: Sly WS]]
-[[Category: Waheed, A.]]
+[[Category: Waheed A]]
-[[Category: Whittington, D A.]]
+[[Category: Whittington DA]]
-[[Category: Alpha-helix]]
-[[Category: Beta-sheet]]
-[[Category: Lyase]]
-[[Category: Zinc enzyme]]