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| | ==Crystal Structure of carbonic anhydrase RV3588c from Mycobacterium tuberculosis== | | ==Crystal Structure of carbonic anhydrase RV3588c from Mycobacterium tuberculosis== |
| - | <StructureSection load='1ym3' size='340' side='right' caption='[[1ym3]], [[Resolution|resolution]] 1.75Å' scene=''> | + | <StructureSection load='1ym3' size='340' side='right'caption='[[1ym3]], [[Resolution|resolution]] 1.75Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1ym3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Myctu Myctu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YM3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1YM3 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1ym3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YM3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YM3 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Rv3588c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 MYCTU])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></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=1ym3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ym3 OCA], [https://pdbe.org/1ym3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ym3 RCSB], [https://www.ebi.ac.uk/pdbsum/1ym3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ym3 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ym3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ym3 OCA], [http://pdbe.org/1ym3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ym3 RCSB], [http://www.ebi.ac.uk/pdbsum/1ym3 PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MTCA2_MYCTO MTCA2_MYCTO]] Catalyzes the reversible hydration of carbon dioxide to form bicarbonate. | + | [https://www.uniprot.org/uniprot/MTCA2_MYCTU MTCA2_MYCTU] Catalyzes the reversible hydration of carbon dioxide to form bicarbonate.<ref>PMID:15753099</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ym/1ym3_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ym/1ym3_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
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| | ==See Also== | | ==See Also== |
| - | *[[Carbonic anhydrase|Carbonic anhydrase]] | + | *[[Carbonic anhydrase 3D structures|Carbonic anhydrase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Carbonate dehydratase]] | + | [[Category: Large Structures]] |
| - | [[Category: Myctu]] | + | [[Category: Mycobacterium tuberculosis H37Rv]] |
| - | [[Category: Bergfors, T]] | + | [[Category: Bergfors T]] |
| - | [[Category: Bjorkelid, C]] | + | [[Category: Bjorkelid C]] |
| - | [[Category: Covarrubias, A S]] | + | [[Category: Covarrubias AS]] |
| - | [[Category: Hogbom, M]] | + | [[Category: Hogbom M]] |
| - | [[Category: Jones, T A]] | + | [[Category: Jones TA]] |
| - | [[Category: Larsson, A M]] | + | [[Category: Larsson AM]] |
| - | [[Category: Lindberg, J]] | + | [[Category: Lindberg J]] |
| - | [[Category: Mowbray, S L]] | + | [[Category: Mowbray SL]] |
| - | [[Category: SPINE, Structural Proteomics in Europe]]
| + | [[Category: Unge T]] |
| - | [[Category: Unge, T]] | + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Spine]]
| + | |
| - | [[Category: Structural genomic]]
| + | |
| - | [[Category: Structural proteomics in europe]]
| + | |
| - | [[Category: Zn protein]]
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| Structural highlights
Function
MTCA2_MYCTU Catalyzes the reversible hydration of carbon dioxide to form bicarbonate.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Carbonic anhydrases catalyze the reversible hydration of carbon dioxide to form bicarbonate. This activity is universally required for fatty acid biosynthesis as well as for the production of a number of small molecules, pH homeostasis, and other functions. At least three different carbonic anhydrase families are known to exist, of which the alpha-class found in humans has been studied in most detail. In the present work, we describe the structures of two of the three beta-class carbonic anhydrases that have been identified in Mycobacterium tuberculosis, i.e. Rv1284 and Rv3588c. Both structures were solved by molecular replacement and then refined to resolutions of 2.0 and 1.75 A, respectively. The active site of Rv1284 is small and almost completely shielded from solvent, whereas that of Rv3588c is larger and quite open to solution. Differences in coordination of the active site metal are also observed. In Rv3588c, an aspartic acid side chain displaces a water molecule and coordinates directly to the zinc ion, thereby closing the zinc coordination sphere and breaking the salt link to a nearby arginine that is a feature of Rv1284. The two carbonic anhydrases thus exhibit both of the metal coordination geometries that have previously been observed for structures in this family. Activity studies demonstrate that Rv3588c is a completely functional carbonic anhydrase. The apparent lack of activity of Rv1284 in the present assay system is likely exacerbated by the observed depletion of zinc in the preparation.
Structure and function of carbonic anhydrases from Mycobacterium tuberculosis.,Suarez Covarrubias A, Larsson AM, Hogbom M, Lindberg J, Bergfors T, Bjorkelid C, Mowbray SL, Unge T, Jones TA J Biol Chem. 2005 May 13;280(19):18782-9. Epub 2005 Mar 6. PMID:15753099[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Suarez Covarrubias A, Larsson AM, Hogbom M, Lindberg J, Bergfors T, Bjorkelid C, Mowbray SL, Unge T, Jones TA. Structure and function of carbonic anhydrases from Mycobacterium tuberculosis. J Biol Chem. 2005 May 13;280(19):18782-9. Epub 2005 Mar 6. PMID:15753099 doi:http://dx.doi.org/10.1074/jbc.M414348200
- ↑ Suarez Covarrubias A, Larsson AM, Hogbom M, Lindberg J, Bergfors T, Bjorkelid C, Mowbray SL, Unge T, Jones TA. Structure and function of carbonic anhydrases from Mycobacterium tuberculosis. J Biol Chem. 2005 May 13;280(19):18782-9. Epub 2005 Mar 6. PMID:15753099 doi:http://dx.doi.org/10.1074/jbc.M414348200
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