4hpx

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{{STRUCTURE_4hpx| PDB=4hpx | SCENE= }}
{{STRUCTURE_4hpx| PDB=4hpx | SCENE= }}
===Crystal structure of Tryptophan Synthase at 1.65 A resolution in complex with alpha aminoacrylate E(A-A) and benzimidazole in the beta site and the F9 inhibitor in the alpha site===
===Crystal structure of Tryptophan Synthase at 1.65 A resolution in complex with alpha aminoacrylate E(A-A) and benzimidazole in the beta site and the F9 inhibitor in the alpha site===
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{{ABSTRACT_PUBMED_23952479}}
==Function==
==Function==
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==About this Structure==
==About this Structure==
[[4hpx]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HPX OCA].
[[4hpx]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HPX OCA].
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==Reference==
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<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 10:49, 1 January 2014

Template:STRUCTURE 4hpx

Contents

Crystal structure of Tryptophan Synthase at 1.65 A resolution in complex with alpha aminoacrylate E(A-A) and benzimidazole 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

4hpx 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:http://dx.doi.org/10.1021/bi400795e

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