2clm: Difference between revisions
New page: left|200px<br /> <applet load="2clm" size="450" color="white" frame="true" align="right" spinBox="true" caption="2clm, resolution 1.51Å" /> '''TRYPTOPHAN SYNTHASE... |
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==About this Structure== | ==About this Structure== | ||
2CLM is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium]] with NA, F6F and PLS as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.20 4.2.1.20]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CLM OCA]]. | 2CLM is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium]] with NA, F6F and PLS as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Tryptophan_synthase Tryptophan synthase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.20 4.2.1.20]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CLM OCA]]. | ||
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Salmonella typhimurium]] | [[Category: Salmonella typhimurium]] | ||
[[Category: Tryptophan synthase]] | |||
[[Category: Barends, T.R.]] | [[Category: Barends, T.R.]] | ||
[[Category: Blumenstein, L.]] | [[Category: Blumenstein, L.]] | ||
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[[Category: tryptophan biosynthesis]] | [[Category: tryptophan biosynthesis]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:17:22 2007'' |
Revision as of 13:12, 30 October 2007
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TRYPTOPHAN SYNTHASE (EXTERNAL ALDIMINE STATE) IN COMPLEX WITH N-(4'-TRIFLUOROMETHOXYBENZOYL)-2-AMINO-1-ETHYLPHOSPHATE (F6F)
OverviewOverview
Allosteric interactions regulate substrate channeling in Salmonella, typhimurium tryptophan synthase. The channeling of indole between the, alpha- and beta-sites via the interconnecting 25 A tunnel is regulated by, allosteric signaling arising from binding of ligand to the alpha-site, and, covalent reaction of l-Ser at the beta-site. This signaling switches the, alpha- and beta-subunits between open conformations of low activity and, closed conformations of high activity. Our objective is to synthesize and, characterize new classes of alpha-site ligands (ASLs) that mimic the, binding of substrates, 3-indole-d-glycerol 3'-phosphate (IGP) or, d-glyceraldehyde 3-phosphate (G3P), for use in the investigation of, alpha-site-beta-site interactions. The new synthesized IGP analogues, contain an ... [(full description)]
About this StructureAbout this Structure
2CLM is a [Protein complex] structure of sequences from [Salmonella typhimurium] with NA, F6F and PLS as [ligands]. Active as [Tryptophan synthase], with EC number [4.2.1.20]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Synthesis and characterization of allosteric probes of substrate channeling in the tryptophan synthase bienzyme complex., Ngo H, Harris R, Kimmich N, Casino P, Niks D, Blumenstein L, Barends TR, Kulik V, Weyand M, Schlichting I, Dunn MF, Biochemistry. 2007 Jul 3;46(26):7713-27. Epub 2007 Jun 9. PMID:17559195
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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
- Protein complex
- Salmonella typhimurium
- Tryptophan synthase
- Barends, T.R.
- Blumenstein, L.
- Dunn, M.F.
- Harris, R.
- Kimmich, N.
- Kulik, V.
- Ngo, H.
- Niks, D.
- Schlichting, I.
- F6F
- NA
- PLS
- Allosteric enzyme
- Amino-acid biosynthesis
- Aromatic amino acid biosynthesis
- Carbon-oxygen lyase
- Lyase
- Pyridoxal phosphate
- Tryptophan biosynthesis