1huh

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[[Image:1huh.jpg|left|200px]]<br /><applet load="1huh" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1huh, resolution 2.2&Aring;" />
 
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'''DIFFERENCES IN ANIONIC INHIBITION OF HUMAN CARBONIC ANHYDRASE I REVEALED FROM THE STRUCTURES OF IODIDE AND GOLD CYANIDE INHIBITOR COMPLEXES'''<br />
 
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==Overview==
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==DIFFERENCES IN ANIONIC INHIBITION OF HUMAN CARBONIC ANHYDRASE I REVEALED FROM THE STRUCTURES OF IODIDE AND GOLD CYANIDE INHIBITOR COMPLEXES==
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The crystal structures of two anionic inhibitor complexes of human, carbonic anhydrase I (HCAI), namely, HCAI-iodide and HCAI-Au(CN)(2)(-), have been refined by the restrained least-squares method at 2.2 and 2 A, nominal resolution, respectively, with good stereochemistry for the final, models. The R values have improved from 30.3 to 16.6% for HCAI-iodide and, from 28.8 to 17.1% for HCAI-Au(CN)(2)(-). The sites of inhibitor binding, as elucidated are totally different in the two structures. The iodide, anion replaces the zinc-bound H(2)O/OH(-) ligand and renders the enzyme, inactive. This result confirms that the zinc-bound H(2)O/OH(-) is the, activity-linked group in carbonic anhydrase enzymes. Au(CN)(2)(-) binds at, a different and new site near the zinc ion, without liganding to the, metal. The N atom of Au(CN)(2)(-) is within hydrogen-bonding distance of, the zinc-bound H(2)O/OH(-) group which shifts by about 0.4 A away from the, zinc ion in relation to its position in the native HCAI. It is proposed, that the presence of the inhibitor Au(CN)(2)(-) results in a, conformational reorientation of the activity-linked group, due to, hydrogen-bond formation with the inhibitor, which in turn sterically, hinders the binding of the substrate CO(2) molecule in the active site, leading to the inhibition of HCAI enzyme.
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<StructureSection load='1huh' size='340' side='right'caption='[[1huh]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1huh]] 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=1HUH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HUH FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1huh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1huh OCA], [https://pdbe.org/1huh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1huh RCSB], [https://www.ebi.ac.uk/pdbsum/1huh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1huh ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CAH1_HUMAN CAH1_HUMAN] Reversible hydration of carbon dioxide. Can hydrates cyanamide to urea.<ref>PMID:10550681</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hu/1huh_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1huh ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1HUH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=IOD:'>IOD</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=1HUH OCA].
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*[[Carbonic anhydrase 3D structures|Carbonic anhydrase 3D structures]]
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== References ==
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==Reference==
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<references/>
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Differences in anionic inhibition of human carbonic anhydrase I revealed from the structures of iodide and gold cyanide inhibitor complexes., Kumar V, Kannan KK, Sathyamurthi P, Acta Crystallogr D Biol Crystallogr. 1994 Sep 1;50(Pt 5):731-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15299369 15299369]
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__TOC__
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[[Category: Carbonate dehydratase]]
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Kannan, K.K.]]
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[[Category: Kannan KK]]
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[[Category: Kumar, V.]]
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[[Category: Kumar V]]
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[[Category: IOD]]
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[[Category: ZN]]
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[[Category: lyase(oxo-acid)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:58:13 2008''
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Current revision

DIFFERENCES IN ANIONIC INHIBITION OF HUMAN CARBONIC ANHYDRASE I REVEALED FROM THE STRUCTURES OF IODIDE AND GOLD CYANIDE INHIBITOR COMPLEXES

PDB ID 1huh

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