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2o0r

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[[Image:2o0r.gif|left|200px]]
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{{STRUCTURE_2o0r| PDB=2o0r | SCENE= }}
{{STRUCTURE_2o0r| PDB=2o0r | SCENE= }}
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'''The three-dimensional structure of N-Succinyldiaminopimelate aminotransferase from Mycobacterium tuberculosis'''
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===The three-dimensional structure of N-Succinyldiaminopimelate aminotransferase from Mycobacterium tuberculosis===
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==Overview==
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Inhibitors of the enzymes of the lysine biosynthetic pathway are considered promising lead compounds for the design of new antibacterial drugs, because the pathway appears to be indispensable for bacteria and because it is absent in humans. As part of our efforts to structurally characterize all enzymes of this pathway in Mycobacterium tuberculosis (Mtb), we have determined the three-dimensional structure of N-succinyldiaminopimelate aminotransferase (DapC, DAP-AT, Rv0858c) to a resolution of 2.0 A. This structure is the first DAP-AT structure reported to date. The orthorhombic crystals of Mtb-DAP-AT contain one functional dimer exhibiting C(2) symmetry in the asymmetric unit. The homodimer displays the typical S-shape of class I pyridoxal-5'-phosphate (PLP)-binding proteins. The two active sites of the dimer both feature an internal aldimine with the co-factor PLP covalently bound to the Lys232, although neither substrate nor co-factor had been added during protein production, purification and crystallization. Nine water molecules are conserved in the active site and form an intricate hydrogen-bonding network with the co-factor and the surrounding amino acid residues. Together with some residual difference electron density in the active site, this architecture permitted the building of external aldimine models of the enzyme with the substrates glutamate, the amine donor, and N-succinyl-2-amino-6-keto-pimelate, the amine acceptor. Based on these models, the amino acids relevant for substrate binding and specificity can be postulated. Furthermore, in the external aldimine model of N-succinyl-2-amino-6-keto-pimelate, the succinyl group overlaps with a glycerol binding site that has also been identified in both active sites of the Mtb-DAP-AT dimer. A comparison of the structure of Mtb-DAP-AT with other class I PLP-binding proteins, revealed that some inhibitors utilize the same binding site. Thus, the proposed models also provide an explanation for the mode of inhibition of Mtb-DAP-AT and they may be of help in the design of compounds, which are capable of inhibiting the enzyme. Last, but not least, a chloride binding helix exhibiting a peculiar amino acid sequence with a number of exposed hydrophobic side-chains was identified, which may be hypothesized as a putative docking site.
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(as it appears on PubMed at http://www.pubmed.gov), where 17292400 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17292400}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
The three-dimensional structure of N-succinyldiaminopimelate aminotransferase from Mycobacterium tuberculosis., Weyand S, Kefala G, Weiss MS, J Mol Biol. 2007 Mar 30;367(3):825-38. Epub 2007 Jan 12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17292400 17292400]
The three-dimensional structure of N-succinyldiaminopimelate aminotransferase from Mycobacterium tuberculosis., Weyand S, Kefala G, Weiss MS, J Mol Biol. 2007 Mar 30;367(3):825-38. Epub 2007 Jan 12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17292400 17292400]
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Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of DapC (Rv0858c) from Mycobacterium tuberculosis., Weyand S, Kefala G, Weiss MS, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Aug 1;62(Pt, 8):794-7. Epub 2006 Jul 25. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16880560 16880560]
[[Category: Mycobacterium tuberculosis]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Tb structural genomics consortium]]
[[Category: Tb structural genomics consortium]]
[[Category: Tbsgc]]
[[Category: Tbsgc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 10:09:41 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 04:55:47 2008''

Revision as of 01:55, 29 July 2008

Image:2o0r.png

Template:STRUCTURE 2o0r

The three-dimensional structure of N-Succinyldiaminopimelate aminotransferase from Mycobacterium tuberculosis

Template:ABSTRACT PUBMED 17292400

About this Structure

2O0R is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.

Reference

The three-dimensional structure of N-succinyldiaminopimelate aminotransferase from Mycobacterium tuberculosis., Weyand S, Kefala G, Weiss MS, J Mol Biol. 2007 Mar 30;367(3):825-38. Epub 2007 Jan 12. PMID:17292400

Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of DapC (Rv0858c) from Mycobacterium tuberculosis., Weyand S, Kefala G, Weiss MS, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Aug 1;62(Pt, 8):794-7. Epub 2006 Jul 25. PMID:16880560

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