1ym3
From Proteopedia
(New page: 200px<br /><applet load="1ym3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ym3, resolution 1.75Å" /> '''Crystal Structure of...) |
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| - | [[Image:1ym3.gif|left|200px]]<br /><applet load="1ym3" size=" | + | [[Image:1ym3.gif|left|200px]]<br /><applet load="1ym3" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ym3, resolution 1.75Å" /> | caption="1ym3, resolution 1.75Å" /> | ||
'''Crystal Structure of carbonic anhydrase RV3588c from Mycobacterium tuberculosis'''<br /> | '''Crystal Structure of carbonic anhydrase RV3588c from Mycobacterium tuberculosis'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Carbonic anhydrases catalyze the reversible hydration of carbon dioxide to | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1YM3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_h37rv Mycobacterium tuberculosis h37rv] with ZN and MG 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:// | + | 1YM3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_h37rv Mycobacterium tuberculosis h37rv] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=MG:'>MG</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=1YM3 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bergfors, T.]] | [[Category: Bergfors, T.]] | ||
[[Category: Bjorkelid, C.]] | [[Category: Bjorkelid, C.]] | ||
| - | [[Category: Covarrubias, A | + | [[Category: Covarrubias, A S.]] |
[[Category: Hogbom, M.]] | [[Category: Hogbom, M.]] | ||
| - | [[Category: Jones, T | + | [[Category: Jones, T A.]] |
| - | [[Category: Larsson, A | + | [[Category: Larsson, A M.]] |
[[Category: Lindberg, J.]] | [[Category: Lindberg, J.]] | ||
| - | [[Category: Mowbray, S | + | [[Category: Mowbray, S L.]] |
| - | [[Category: SPINE, Structural | + | [[Category: SPINE, Structural Proteomics in Europe.]] |
[[Category: Unge, T.]] | [[Category: Unge, T.]] | ||
[[Category: MG]] | [[Category: MG]] | ||
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[[Category: zn protein]] | [[Category: zn protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:06:44 2008'' |
Revision as of 14:06, 21 February 2008
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Crystal Structure of carbonic anhydrase RV3588c from Mycobacterium tuberculosis
Overview
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.
About this Structure
1YM3 is a Single protein structure of sequence from Mycobacterium tuberculosis h37rv with and as ligands. Active as Carbonate dehydratase, with EC number 4.2.1.1 Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 16:06:44 2008
Categories: Carbonate dehydratase | Mycobacterium tuberculosis h37rv | Single protein | Bergfors, T. | Bjorkelid, C. | Covarrubias, A S. | Hogbom, M. | Jones, T A. | Larsson, A M. | Lindberg, J. | Mowbray, S L. | SPINE, Structural Proteomics in Europe. | Unge, T. | MG | ZN | Spine | Structural genomics | Structural proteomics in europe | Zn protein
