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1a50

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[[Image:1a50.png|left|200px]]
 
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{{STRUCTURE_1a50| PDB=1a50 | SCENE= }}
{{STRUCTURE_1a50| PDB=1a50 | SCENE= }}
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===CRYSTAL STRUCTURE OF WILD-TYPE TRYPTOPHAN SYNTHASE COMPLEXED WITH 5-FLUOROINDOLE PROPANOL PHOSPHATE===
===CRYSTAL STRUCTURE OF WILD-TYPE TRYPTOPHAN SYNTHASE COMPLEXED WITH 5-FLUOROINDOLE PROPANOL PHOSPHATE===
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{{ABSTRACT_PUBMED_9548921}}
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==Function==
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[[http://www.uniprot.org/uniprot/TRPA_SALTY TRPA_SALTY]] The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. [[http://www.uniprot.org/uniprot/TRPB_SALTY TRPB_SALTY]] The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
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{{ABSTRACT_PUBMED_9548921}}
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==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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<ref group="xtra">PMID:009548921</ref><references group="xtra"/>
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<ref group="xtra">PMID:009548921</ref><references group="xtra"/><references/>
[[Category: Salmonella enterica subsp. enterica serovar typhimurium]]
[[Category: Salmonella enterica subsp. enterica serovar typhimurium]]
[[Category: Tryptophan synthase]]
[[Category: Tryptophan synthase]]

Revision as of 06:34, 10 April 2014

Template:STRUCTURE 1a50

Contents

CRYSTAL STRUCTURE OF WILD-TYPE TRYPTOPHAN SYNTHASE COMPLEXED WITH 5-FLUOROINDOLE PROPANOL PHOSPHATE

Template:ABSTRACT PUBMED 9548921

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

1a50 is a 2 chain structure with sequence from Salmonella enterica subsp. enterica serovar typhimurium. Full crystallographic information is available from OCA.

Reference

  • Schneider TR, Gerhardt E, Lee M, Liang PH, Anderson KS, Schlichting I. Loop closure and intersubunit communication in tryptophan synthase. Biochemistry. 1998 Apr 21;37(16):5394-406. PMID:9548921 doi:http://dx.doi.org/10.1021/bi9728957

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OCA

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