1ztb
From Proteopedia
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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. Active as Chorismate synthase, with EC number 4.2.3.5 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 Wed Nov 21 07:38:52 2007
