1ztb
From Proteopedia
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[[Image:1ztb.gif|left|200px]] | [[Image:1ztb.gif|left|200px]] | ||
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'''Crystal Structure of Chorismate Synthase from Mycobacterium tuberculosis''' | '''Crystal Structure of Chorismate Synthase from Mycobacterium tuberculosis''' | ||
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[[Category: Ramos, C H.I.]] | [[Category: Ramos, C H.I.]] | ||
[[Category: Santos, D S.]] | [[Category: Santos, D S.]] | ||
- | [[Category: | + | [[Category: Beta-alpha-beta]] |
- | [[Category: | + | [[Category: Flavoprotein]] |
- | [[Category: | + | [[Category: Shikimate]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:02:46 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 15:02, 3 May 2008
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1ztb, resolution 2.65Å () | |||||||||
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Gene: | aroC, aroF (Mycobacterium tuberculosis) | ||||||||
Activity: | Chorismate synthase, with EC number 4.2.3.5 | ||||||||
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Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||
Coordinates: | save as pdb, mmCIF, xml |
Crystal Structure of Chorismate Synthase from Mycobacterium tuberculosis
Overview
In bacteria, fungi, plants, and apicomplexan parasites, the aromatics compounds, such as aromatics amino acids, are synthesized through seven enzymes from the shikimate pathway, which are absent in mammals. The absence of this pathway in mammals make them potential targets for development of new therapy against infectious diseases, such as tuberculosis, which is the world's second commonest cause of death from infectious disease. The last enzyme of shikimate pathway is the chorismate synthase (CS), which is responsible for conversion of the 5-enolpyruvylshikimate-3-phosphate to chorismate. Here, we report the crystallographic structure of CS from Mycobacterium tuberculosis (MtCS) at 2.65 A resolution. The MtCS structure is similar to other CS structures, presenting beta-alpha-beta sandwich structural topology, in which each monomer of MtCS consists of a central helical core. The MtCS can be described as a tetramer formed by a dimer of dimers. However, analytical ultracentrifugation studies suggest the MtCS is a dimer with a more asymmetric shape than observed on the crystallographic dimer and the existence of a low equilibrium between dimer and tetramer. Our results suggest that the MtCS oligomerization is concentration dependent and some conformational changes must be involved on that event.
About this Structure
1ZTB is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.
Reference
Structure of chorismate synthase from Mycobacterium tuberculosis., Dias MV, Borges JC, Ely F, Pereira JH, Canduri F, Ramos CH, Frazzon J, Palma MS, Basso LA, Santos DS, de Azevedo WF Jr, J Struct Biol. 2006 May;154(2):130-43. Epub 2006 Jan 17. PMID:16459102 Page seeded by OCA on Sat May 3 18:02:46 2008