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| - | [[Image:2a5v.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:2a5v.png|left|200px]] |
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| | {{STRUCTURE_2a5v| PDB=2a5v | SCENE= }} | | {{STRUCTURE_2a5v| PDB=2a5v | SCENE= }} |
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| - | '''Crystal structure of M. tuberculosis beta carbonic anhydrase, Rv3588c, tetrameric form'''
| + | ===Crystal structure of M. tuberculosis beta carbonic anhydrase, Rv3588c, tetrameric form=== |
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| - | ==Overview==
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| - | Carbonic anhydrases catalyze the reversible hydration of carbon dioxide to form bicarbonate, a reaction required for many functions, including carbon assimilation and pH homeostasis. Carbonic anhydrases are divided into at least three classes and are believed to share a zinc-hydroxide mechanism for carbon dioxide hydration. beta-carbonic anhydrases are broadly spread among the domains of life, and existing structures from different organisms show two distinct active site setups, one with three protein coordinations to the zinc (accessible) and the other with four (blocked). The latter is believed to be inconsistent with the zinc-hydroxide mechanism. The Mycobacterium tuberculosis Rv3588c gene, shown to be required for in vivo growth of the pathogen, encodes a beta-carbonic anhydrase with a steep pH dependence of its activity, being active at pH 8.4 but not at pH 7.5. We have recently solved the structure of this protein, which was a dimeric protein with a blocked active site. Here we present the structure of the thiocyanate complexed protein in a different crystal form. The protein now forms distinct tetramers and shows large structural changes, including a carboxylate shift yielding the accessible active site. This structure demonstrated for the first time that a beta-carbonic anhydrase can switch between the two states. A pH-dependent dimer to tetramer equilibrium was also demonstrated by dynamic light scattering measurements. The data presented here, therefore, suggest a carboxylate shift on/off switch for the enzyme, which may, in turn, be controlled by a dimer-to-tetramer equilibrium.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_16321983}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16321983 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_16321983}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Tetramer]] | | [[Category: Tetramer]] |
| | [[Category: Zinc]] | | [[Category: Zinc]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:38:42 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:07:25 2008'' |
Revision as of 10:07, 29 July 2008
Template:STRUCTURE 2a5v
Crystal structure of M. tuberculosis beta carbonic anhydrase, Rv3588c, tetrameric form
Template:ABSTRACT PUBMED 16321983
About this Structure
2A5V is a Single protein structure of sequence from Mycobacterium tuberculosis h37rv. Full crystallographic information is available from OCA.
Reference
Structural mechanics of the pH-dependent activity of beta-carbonic anhydrase from Mycobacterium tuberculosis., Covarrubias AS, Bergfors T, Jones TA, Hogbom M, J Biol Chem. 2006 Feb 24;281(8):4993-9. Epub 2005 Dec 1. PMID:16321983
Page seeded by OCA on Tue Jul 29 13:07:25 2008
