2bpq
From Proteopedia
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| - | [[Image:2bpq.gif|left|200px]] | + | [[Image:2bpq.gif|left|200px]] |
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| - | '''ANTHRANILATE PHOSPHORIBOSYLTRANSFERASE (TRPD) FROM MYCOBACTERIUM TUBERCULOSIS (APO STRUCTURE)''' | + | {{Structure |
| + | |PDB= 2bpq |SIZE=350|CAPTION= <scene name='initialview01'>2bpq</scene>, resolution 1.90Å | ||
| + | |SITE= <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+A'>AC1</scene> | ||
| + | |LIGAND= <scene name='pdbligand=BEN:BENZAMIDINE'>BEN</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Anthranilate_phosphoribosyltransferase Anthranilate phosphoribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.18 2.4.2.18] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''ANTHRANILATE PHOSPHORIBOSYLTRANSFERASE (TRPD) FROM MYCOBACTERIUM TUBERCULOSIS (APO STRUCTURE)''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2BPQ is a [ | + | 2BPQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BPQ OCA]. |
==Reference== | ==Reference== | ||
| - | The crystal structure of TrpD, a metabolic enzyme essential for lung colonization by Mycobacterium tuberculosis, in complex with its substrate phosphoribosylpyrophosphate., Lee CE, Goodfellow C, Javid-Majd F, Baker EN, Shaun Lott J, J Mol Biol. 2006 Jan 27;355(4):784-97. Epub 2005 Nov 22. PMID:[http:// | + | The crystal structure of TrpD, a metabolic enzyme essential for lung colonization by Mycobacterium tuberculosis, in complex with its substrate phosphoribosylpyrophosphate., Lee CE, Goodfellow C, Javid-Majd F, Baker EN, Shaun Lott J, J Mol Biol. 2006 Jan 27;355(4):784-97. Epub 2005 Nov 22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16337227 16337227] |
[[Category: Anthranilate phosphoribosyltransferase]] | [[Category: Anthranilate phosphoribosyltransferase]] | ||
[[Category: Mycobacterium tuberculosis]] | [[Category: Mycobacterium tuberculosis]] | ||
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[[Category: protein structure initiative]] | [[Category: protein structure initiative]] | ||
[[Category: psi]] | [[Category: psi]] | ||
| - | [[Category: structural | + | [[Category: structural genomic]] |
[[Category: tb structural genomics consortium]] | [[Category: tb structural genomics consortium]] | ||
[[Category: tbsgc]] | [[Category: tbsgc]] | ||
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[[Category: tryptophan biosynthesis]] | [[Category: tryptophan biosynthesis]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:05:00 2008'' |
Revision as of 14:05, 20 March 2008
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| , resolution 1.90Å | |||||||
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| Sites: | |||||||
| Ligands: | and | ||||||
| Activity: | Anthranilate phosphoribosyltransferase, with EC number 2.4.2.18 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ANTHRANILATE PHOSPHORIBOSYLTRANSFERASE (TRPD) FROM MYCOBACTERIUM TUBERCULOSIS (APO STRUCTURE)
Overview
Mycobacterium tuberculosis, the cause of tuberculosis, presents a major threat to human health worldwide. Biosynthetic enzymes that are essential for the survival of the bacterium, especially in activated macrophages, are important potential drug targets. Although the tryptophan biosynthesis pathway is thought to be non-essential for many pathogens, this appears not to be the case for M.tuberculosis, where a trpD gene knockout fails to cause disease in mice. We therefore chose the product of the trpD gene, anthranilate phosphoribosyltransferase, which catalyses the second step in tryptophan biosynthesis, for structural analysis. The structure of TrpD from M.tuberculosis was solved by X-ray crystallography, at 1.9 A resolution for the native enzyme (R = 0.191, Rfree = 0.230) and at 2.3 A resolution for the complex with its substrate phosphoribosylpyrophosphate (PRPP) and Mg2+ (R = 0.194, Rfree = 0.255). The enzyme is folded into two domains, separated by a hinge region. PRPP binds in the C-terminal domain, together with a pair of Mg ions. In the substrate complex, two flexible loops change conformation compared with the apo protein, to close over the PRPP and to complete an extensive network of hydrogen-bonded interactions. A nearby pocket, adjacent to the hinge region, is postulated by in silico docking as the binding site for anthranilate. A bound molecule of benzamidine, which was essential for crystallization and is also found in the hinge region, appears to reduce flexibility between the two domains.
About this Structure
2BPQ is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.
Reference
The crystal structure of TrpD, a metabolic enzyme essential for lung colonization by Mycobacterium tuberculosis, in complex with its substrate phosphoribosylpyrophosphate., Lee CE, Goodfellow C, Javid-Majd F, Baker EN, Shaun Lott J, J Mol Biol. 2006 Jan 27;355(4):784-97. Epub 2005 Nov 22. PMID:16337227
Page seeded by OCA on Thu Mar 20 16:05:00 2008
Categories: Anthranilate phosphoribosyltransferase | Mycobacterium tuberculosis | Single protein | Baker, E N. | Goodfellow, C. | Javid-Majd, F. | Lee, C E. | Lott, J S. | TBSGC, TB Structural Genomics Consortium. | BEN | GOL | Amino-acid biosynthesis | Anthranilate | Aromatic amino acid biosynthesis | Glycosyltransferase | Protein structure initiative | Psi | Structural genomic | Tb structural genomics consortium | Tbsgc | Transferase phosphoribosyltransferase | Tryptophan biosynthesis
