4hpj: Difference between revisions
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{{STRUCTURE_4hpj| PDB=4hpj | SCENE= }} | {{STRUCTURE_4hpj| PDB=4hpj | SCENE= }} | ||
===Crystal structure of Tryptophan Synthase at 1.45 A resolution in complex with 2-aminophenol quinonoid in the beta site and the F9 inhibitor in the alpha site=== | ===Crystal structure of Tryptophan Synthase at 1.45 A resolution in complex with 2-aminophenol quinonoid in the beta site and the F9 inhibitor in the alpha site=== | ||
{{ABSTRACT_PUBMED_23952479}} | |||
==Function== | ==Function== | ||
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==About this Structure== | ==About this Structure== | ||
[[4hpj]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HPJ OCA]. | [[4hpj]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HPJ OCA]. | ||
==Reference== | |||
<ref group="xtra">PMID:023952479</ref><references group="xtra"/><references/> | |||
[[Category: Tryptophan synthase]] | [[Category: Tryptophan synthase]] | ||
[[Category: Dunn, M F.]] | [[Category: Dunn, M F.]] | ||
Revision as of 10:55, 1 January 2014
Crystal structure of Tryptophan Synthase at 1.45 A resolution in complex with 2-aminophenol quinonoid in the beta site and the F9 inhibitor in the alpha site
Template:ABSTRACT PUBMED 23952479
Function
[TRPA_SALTY] The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. [TRPB_SALTY] The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
About this Structure
4hpj is a 2 chain structure. Full crystallographic information is available from OCA.
Reference
- Niks D, Hilario E, Dierkers A, Ngo H, Borchardt D, Neubauer TJ, Fan L, Mueller LJ, Dunn MF. Allostery and substrate channeling in the tryptophan synthase bienzyme complex: evidence for two subunit conformations and four quaternary states. Biochemistry. 2013 Sep 17;52(37):6396-411. doi: 10.1021/bi400795e. Epub 2013 Sep , 6. PMID:23952479 doi:https://dx.doi.org/10.1021/bi400795e
