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1qrm

From Proteopedia

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[[Image:1qrm.gif|left|200px]]
 
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{{Structure
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==A CLOSER LOOK AT THE ACTIVE SITE OF GAMMA-CARBONIC ANHYDRASES: HIGH RESOLUTION CRYSTAL STRUCTURES OF THE CARBONIC ANHYDRASE FROM METHANOSARCINA THERMOPHILA==
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|PDB= 1qrm |SIZE=350|CAPTION= <scene name='initialview01'>1qrm</scene>, resolution 1.95&Aring;
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<StructureSection load='1qrm' size='340' side='right'caption='[[1qrm]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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<table><tr><td colspan='2'>[[1qrm]] 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=1QRM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QRM FirstGlance]. <br>
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|ACTIVITY=
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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]] 1.95&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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|DOMAIN=
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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=1qrm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qrm OCA], [https://pdbe.org/1qrm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qrm RCSB], [https://www.ebi.ac.uk/pdbsum/1qrm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qrm ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1thj|1thj]], [[1qq0|1qq0]], [[1qre|1qre]], [[1qrf|1qrf]], [[1qrg|1qrg]], [[1qrl|1qrl]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qrm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qrm OCA], [http://www.ebi.ac.uk/pdbsum/1qrm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qrm RCSB]</span>
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== Function ==
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}}
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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/1qrm_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=1qrm ConSurf].
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<div style="clear:both"></div>
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'''A CLOSER LOOK AT THE ACTIVE SITE OF GAMMA-CARBONIC ANHYDRASES: HIGH RESOLUTION CRYSTAL STRUCTURES OF THE CARBONIC ANHYDRASE FROM METHANOSARCINA THERMOPHILA'''
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==See Also==
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*[[Carbonic anhydrase 3D structures|Carbonic anhydrase 3D structures]]
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== References ==
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==Overview==
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<references/>
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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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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1QRM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Methanosarcina_thermophila Methanosarcina thermophila]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QRM OCA].
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==Reference==
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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://www.ncbi.nlm.nih.gov/pubmed/10924115 10924115]
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[[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: beta-helix]]
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[[Category: lyase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:18:01 2008''
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Current revision

A CLOSER LOOK AT THE ACTIVE SITE OF GAMMA-CARBONIC ANHYDRASES: HIGH RESOLUTION CRYSTAL STRUCTURES OF THE CARBONIC ANHYDRASE FROM METHANOSARCINA THERMOPHILA

PDB ID 1qrm

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