1ztb

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(New page: 200px<br /><applet load="1ztb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ztb, resolution 2.65&Aring;" /> '''Crystal Structure of...)
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caption="1ztb, resolution 2.65&Aring;" />
caption="1ztb, resolution 2.65&Aring;" />
'''Crystal Structure of Chorismate Synthase from Mycobacterium tuberculosis'''<br />
'''Crystal Structure of Chorismate Synthase from Mycobacterium tuberculosis'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1ZTB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Active as [http://en.wikipedia.org/wiki/Chorismate_synthase Chorismate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.3.5 4.2.3.5] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ZTB OCA].
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1ZTB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Active as [http://en.wikipedia.org/wiki/Chorismate_synthase Chorismate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.3.5 4.2.3.5] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZTB OCA].
==Reference==
==Reference==
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[[Category: Mycobacterium tuberculosis]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Basso, L.A.]]
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[[Category: Basso, L A.]]
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[[Category: Borges, J.C.]]
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[[Category: Borges, J C.]]
[[Category: Canduri, F.]]
[[Category: Canduri, F.]]
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[[Category: Dias, M.V.B.]]
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[[Category: Dias, M V.B.]]
[[Category: Ely, F.]]
[[Category: Ely, F.]]
[[Category: Frazzon, J.]]
[[Category: Frazzon, J.]]
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[[Category: Jr., W.F.Azevedo.]]
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[[Category: Jr., W F.Azevedo.]]
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[[Category: Palma, M.S.]]
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[[Category: Palma, M S.]]
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[[Category: Pereira, J.H.]]
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[[Category: Pereira, J H.]]
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[[Category: Ramos, C.H.I.]]
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[[Category: Ramos, C H.I.]]
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[[Category: Santos, D.S.]]
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[[Category: Santos, D S.]]
[[Category: beta-alpha-beta]]
[[Category: beta-alpha-beta]]
[[Category: flavoprotein]]
[[Category: flavoprotein]]
[[Category: shikimate]]
[[Category: shikimate]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:18:51 2008''

Revision as of 14:18, 21 February 2008


1ztb, resolution 2.65Å

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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

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