1qrg

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(New page: 200px<br /><applet load="1qrg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qrg, resolution 1.72&Aring;" /> '''A CLOSER LOOK AND TH...)
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[[Image:1qrg.gif|left|200px]]<br /><applet load="1qrg" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1qrg, resolution 1.72&Aring;" />
 
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'''A CLOSER LOOK AND THE ACTIVE SITE OF GAMMA-CARBONIC ANHYDRASES: HIGH RESOLUTION CRYSTALLOGRAPHIC STUDIES OF THE CARBONIC ANHYDRASE FROM METHANOSARCINA THERMOPHILA'''<br />
 
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==Overview==
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==A CLOSER LOOK AND THE ACTIVE SITE OF GAMMA-CARBONIC ANHYDRASES: HIGH RESOLUTION CRYSTALLOGRAPHIC STUDIES OF THE CARBONIC ANHYDRASE FROM METHANOSARCINA THERMOPHILA==
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The prototype of the gamma-class of carbonic anhydrase has been, characterized from the methanogenic archaeon Methanosarcina thermophila., Previously reported kinetic studies of the gamma-class carbonic anhydrase, are consistent with this enzyme having a reaction mechanism similar to, that of the mammalian alpha-class carbonic anhydrase. However, the overall, folds of these two enzymes are dissimilar, and apart from the, zinc-coordinating histidines, the active site residues bear little, resemblance to one another. The crystal structures of zinc-containing and, cobalt-substituted gamma-class carbonic anhydrases from M. thermophila are, reported here between 1.46 and 1.95 A resolution in the unbound form and, cocrystallized with either SO(4)(2)(-) or HCO(3)(-). Relative to the, tetrahedral coordination geometry seen at the active site in the, alpha-class of carbonic anhydrases, the active site of the gamma-class, enzyme contains additional metal-bound water ligands, so the overall, coordination geometry is trigonal bipyramidal for the zinc-containing, enzyme and octahedral for the cobalt-substituted enzyme. Ligands bound to, the active site all make contacts with the side chain of Glu 62 in manners, that suggest the side chain is likely protonated. In the uncomplexed, zinc-containing enzyme, the side chains of Glu 62 and Glu 84 appear to, share a proton; additionally, Glu 84 exhibits multiple conformations. This, suggests that Glu 84 may act as a proton shuttle, which is an important, aspect of the reaction mechanism of alpha-class carbonic anhydrases. A, hydrophobic pocket on the surface of the enzyme may participate in the, trapping of CO(2) at the active site. On the basis of the coordination, geometry at the active site, ligand binding modes, the behavior of the, side chains of Glu 62 and Glu 84, and analogies to the well-characterized, alpha-class of carbonic anhydrases, a more-defined reaction mechanism is, proposed for the gamma-class of carbonic anhydrases.
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<StructureSection load='1qrg' size='340' side='right'caption='[[1qrg]], [[Resolution|resolution]] 1.72&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1qrg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanosarcina_thermophila Methanosarcina thermophila]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QRG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QRG 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]] 1.72&#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=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=1qrg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qrg OCA], [https://pdbe.org/1qrg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qrg RCSB], [https://www.ebi.ac.uk/pdbsum/1qrg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qrg ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CAH_METTT CAH_METTT] Reversible hydration of carbon dioxide. Important for growth on acetate (PubMed:8041719). As a probably extracellular enzyme, it may support a H(+)/CH(3)COO(-) symport mechanism and/or conversion of CO(2) to HCO(3)(-), removing excess CO(2) produced by growth on acetate (Probable).<ref>PMID:8041719</ref> <ref>PMID:10924115</ref> <ref>PMID:8041719</ref> <ref>PMID:8665839</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/qr/1qrg_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=1qrg 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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1QRG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanosarcina_thermophila Methanosarcina thermophila] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QRG 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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A closer look at the active site of gamma-class carbonic anhydrases: high-resolution crystallographic studies of the carbonic anhydrase from Methanosarcina thermophila., Iverson TM, Alber BE, Kisker C, Ferry JG, Rees DC, Biochemistry. 2000 Aug 8;39(31):9222-31. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10924115 10924115]
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Methanosarcina thermophila]]
[[Category: Methanosarcina thermophila]]
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[[Category: Single protein]]
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[[Category: Alber BE]]
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[[Category: Alber, B.E.]]
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[[Category: Ferry JG]]
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[[Category: Ferry, J.G.]]
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[[Category: Iverson TM]]
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[[Category: Iverson, T.M.]]
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[[Category: Kisker C]]
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[[Category: Kisker, C.]]
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[[Category: Rees DC]]
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[[Category: Rees, D.C.]]
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[[Category: ZN]]
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[[Category: beta-helix]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:55:05 2007''
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Current revision

A CLOSER LOOK AND THE ACTIVE SITE OF GAMMA-CARBONIC ANHYDRASES: HIGH RESOLUTION CRYSTALLOGRAPHIC STUDIES OF THE CARBONIC ANHYDRASE FROM METHANOSARCINA THERMOPHILA

PDB ID 1qrg

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