1ylk: Difference between revisions

Revision as of 06:04, 28 July 2008

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File:1ylk.png

Template:STRUCTURE 1ylk

Crystal Structure of Rv1284 from Mycobacterium tuberculosis in Complex with ThiocyanateCrystal Structure of Rv1284 from Mycobacterium tuberculosis in Complex with Thiocyanate

Template:ABSTRACT PUBMED 15753099

About this StructureAbout this Structure

1YLK is a Single protein structure of sequence from Mycobacterium tuberculosis h37rv. Full crystallographic information is available from OCA.

ReferenceReference

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

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OCA

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-'''Crystal Structure of Rv1284 from Mycobacterium tuberculosis in Complex with Thiocyanate'''
+===Crystal Structure of Rv1284 from Mycobacterium tuberculosis in Complex with Thiocyanate===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_15753099}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_15753099}}
 ==About this Structure==
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 [[Category: Structural genomic]]
 [[Category: Structural proteomics in europe]]
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