2bpq: Difference between revisions
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==About this Structure== | ==About this Structure== | ||
2BPQ is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]] with BEN and GOL as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ | 2BPQ is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]] with BEN and GOL as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[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]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.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://ispc.weizmann.ac.il//pmbin/getpm?pmid=16337227 16337227] | 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://ispc.weizmann.ac.il//pmbin/getpm?pmid=16337227 16337227] | ||
[[Category: Anthranilate phosphoribosyltransferase]] | |||
[[Category: Mycobacterium tuberculosis]] | [[Category: Mycobacterium tuberculosis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: tryptophan biosynthesis]] | [[Category: tryptophan biosynthesis]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:40:59 2007'' |
Revision as of 11:36, 30 October 2007
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ANTHRANILATE PHOSPHORIBOSYLTRANSFERASE (TRPD) FROM MYCOBACTERIUM TUBERCULOSIS (APO STRUCTURE)
OverviewOverview
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 ... [(full description)]
About this StructureAbout this Structure
2BPQ is a [Single protein] structure of sequence from [Mycobacterium tuberculosis] with BEN and GOL as [ligands]. Active as [Anthranilate phosphoribosyltransferase], with EC number [2.4.2.18]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
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
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Pages with broken file links
- 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 genomics
- Tb structural genomics consortium
- Tbsgc
- Transferase phosphoribosyltransferase
- Tryptophan biosynthesis