1ylk: Difference between revisions
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==Crystal Structure of Rv1284 from Mycobacterium tuberculosis in Complex with Thiocyanate== | |||
<StructureSection load='1ylk' size='340' side='right'caption='[[1ylk]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1ylk]] is a 4 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=1YLK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YLK FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SCN:THIOCYANATE+ION'>SCN</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=1ylk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ylk OCA], [https://pdbe.org/1ylk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ylk RCSB], [https://www.ebi.ac.uk/pdbsum/1ylk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ylk ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/MTCA1_MYCTU MTCA1_MYCTU] Catalyzes the reversible hydration of carbon dioxide to form bicarbonate.<ref>PMID:19317447</ref> | |||
== 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/yl/1ylk_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=1ylk ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:15753099</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1ylk" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
== | __TOC__ | ||
< | </StructureSection> | ||
[[Category: Mycobacterium tuberculosis]] | [[Category: Large Structures]] | ||
[[Category: Bergfors | [[Category: Mycobacterium tuberculosis H37Rv]] | ||
[[Category: Bjorkelid | [[Category: Bergfors T]] | ||
[[Category: Covarrubias | [[Category: Bjorkelid C]] | ||
[[Category: Hogbom | [[Category: Covarrubias AS]] | ||
[[Category: Jones | [[Category: Hogbom M]] | ||
[[Category: Larsson | [[Category: Jones TA]] | ||
[[Category: Lindberg | [[Category: Larsson AM]] | ||
[[Category: Mowbray | [[Category: Lindberg J]] | ||
[[Category: Mowbray SL]] | |||
[[Category: Unge | [[Category: Unge T]] | ||
Latest revision as of 09:58, 23 August 2023
Crystal Structure of Rv1284 from Mycobacterium tuberculosis in Complex with ThiocyanateCrystal Structure of Rv1284 from Mycobacterium tuberculosis in Complex with Thiocyanate
Structural highlights
FunctionMTCA1_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 PubMedCarbonic 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. References
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