1z93: Difference between revisions

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-{{Seed}}
-[[Image:1z93.png|left|200px]]
-<!--
+==Human Carbonic Anhydrase III:Structural and Kinetic study of Catalysis and Proton Transfer.==
-The line below this paragraph, containing "STRUCTURE_1z93", creates the "Structure Box" on the page.
+<StructureSection load='1z93' size='340' side='right'caption='[[1z93]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1z93]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z93 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Z93 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-{{STRUCTURE_1z93|  PDB=1z93  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1z93 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z93 OCA], [https://pdbe.org/1z93 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1z93 RCSB], [https://www.ebi.ac.uk/pdbsum/1z93 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1z93 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/CAH3_HUMAN CAH3_HUMAN] 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/z9/1z93_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1z93 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The residue phenylalanine 198 (Phe 198) is a prominent cause of the lower activity of human carbonic anhydrase III (HCA III) compared with HCA II and other isozymes which have leucine at this site. We report the crystal structures of HCA III and the site-directed mutant F198L HCA III, both at 2.1 A resolution, and the enhancement of catalytic activity by exogenous proton donors containing imidazole rings. Both enzymes had a hexahistidine extension at the carboxy-terminal end, used to aid in purification, that was ordered in the crystal structures bound in the active site cavity of an adjacent symmetry-related enzyme. This observation allowed us to comment on a number of possible binding sites for imidazole and derivatives as exogenous proton donors/acceptors in catalysis by HCA III. Kinetic and structural evidence indicates that the phenyl side chain of Phe 198 in HCA III, about 5 A from the zinc, is a steric constriction in the active site, may cause altered interactions at the zinc-bound solvent, and is a binding site for the activation of catalysis by histidylhistidine. This suggests that sites of activation of the proton-transfer pathway in carbonic anhydrase are closer to the zinc than considered in previous studies.
-===Human Carbonic Anhydrase III:Structural and Kinetic study of Catalysis and Proton Transfer.===
+Human carbonic anhydrase III: structural and kinetic study of catalysis and proton transfer.,Duda DM, Tu C, Fisher SZ, An H, Yoshioka C, Govindasamy L, Laipis PJ, Agbandje-McKenna M, Silverman DN, McKenna R Biochemistry. 2005 Aug 2;44(30):10046-53. PMID:16042381<ref>PMID:16042381</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1z93" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_16042381}}, adds the Publication Abstract to the page
+*[[Carbonic anhydrase 3D structures|Carbonic anhydrase 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 16042381 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_16042381}}
+__TOC__
+</StructureSection>
-==About this Structure==
-Z93 is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z93 OCA].
-==Reference==
-<ref group="xtra">PMID:16042381</ref><references group="xtra"/>
-[[Category: Carbonate dehydratase]]
 [[Category: Homo sapiens]]
-[[Category: Agbandje-McKenna, M.]]
+[[Category: Large Structures]]
-[[Category: An, H.]]
+[[Category: Agbandje-McKenna M]]
-[[Category: Duda, D M.]]
+[[Category: An H]]
-[[Category: Fisher, S Z.]]
+[[Category: Duda DM]]
-[[Category: Govindasamy, L.]]
+[[Category: Fisher SZ]]
-[[Category: Laipis, P J.]]
+[[Category: Govindasamy L]]
-[[Category: McKenna, R.]]
+[[Category: Laipis PJ]]
-[[Category: Silverman, D N.]]
+[[Category: McKenna R]]
-[[Category: Tu, C.]]
+[[Category: Silverman DN]]
-[[Category: Yoshioka, C.]]
+[[Category: Tu C]]
-[[Category: Carbonic anhydrase iii]]
+[[Category: Yoshioka C]]
-[[Category: Chemical rescue]]
-[[Category: Proton wire]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 18:36:20 2009''