2clo: Difference between revisions

Revision as of 05:23, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2clo.png

Template:STRUCTURE 2clo

TRYPTOPHAN SYNTHASE (EXTERNAL ALDIMINE STATE) IN COMPLEX WITH (NAPHTHALENE-2'-SULFONYL)-2-AMINO-1-ETHYLPHOSPHATE (F19)TRYPTOPHAN SYNTHASE (EXTERNAL ALDIMINE STATE) IN COMPLEX WITH (NAPHTHALENE-2'-SULFONYL)-2-AMINO-1-ETHYLPHOSPHATE (F19)

Template:ABSTRACT PUBMED 17559232

About this StructureAbout this Structure

2CLO is a Protein complex structure of sequences from Salmonella typhimurium. Full crystallographic information is available from OCA.

ReferenceReference

Allosteric regulation of substrate channeling in tryptophan synthase: modulation of the L-serine reaction in stage I of the beta-reaction by alpha-site ligands., Ngo H, Kimmich N, Harris R, Niks D, Blumenstein L, Kulik V, Barends TR, Schlichting I, Dunn MF, Biochemistry. 2007 Jul 3;46(26):7740-53. Epub 2007 Jun 9. PMID:17559232

Page seeded by OCA on Tue Jul 29 05:23:30 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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 {{STRUCTURE_2clo|  PDB=2clo  |  SCENE=  }}
-'''TRYPTOPHAN SYNTHASE (EXTERNAL ALDIMINE STATE) IN COMPLEX WITH (NAPHTHALENE-2'-SULFONYL)-2-AMINO-1-ETHYLPHOSPHATE (F19)'''
+===TRYPTOPHAN SYNTHASE (EXTERNAL ALDIMINE STATE) IN COMPLEX WITH (NAPHTHALENE-2'-SULFONYL)-2-AMINO-1-ETHYLPHOSPHATE (F19)===
-==Overview==
+<!--
-In the tryptophan synthase bienzyme complex, indole produced by substrate cleavage at the alpha-site is channeled to the beta-site via a 25 A long tunnel. Within the beta-site, indole and l-Ser react with pyridoxal 5'-phosphate in a two-stage reaction to give l-Trp. In stage I, l-Ser forms an external aldimine, E(Aex1), which converts to the alpha-aminoacrylate aldimine, E(A-A). Formation of E(A-A) at the beta-site activates the alpha-site &gt;30-fold. In stage II, indole reacts with E(A-A) to give l-Trp. The binding of alpha-site ligands (ASLs) exerts strong allosteric effects on the reaction of substrates at the beta-site: the distribution of intermediates formed in stage I is shifted in favor of E(A-A), and the binding of ASLs triggers a conformational change in the beta-site to a state with an increased affinity for l-Ser. Here, we compare the behavior of new ASLs as allosteric effectors of stage I with the behavior of the natural product, d-glyceraldehyde 3-phosphate. Rapid kinetics and kinetic isotope effects show these ASLs bind with affinities ranging from micro- to millimolar, and the rate-determining step for conversion of E(Aex1) to E(A-A) is increased by 8-10-fold. To derive a structure-based mechanism for stage I, X-ray structures of both the E(Aex1) and E(A-A) states complexed with the different ASLs were determined and compared with structures of the ASL complexes with the internal aldimine [Ngo, H., Harris, R., Kimmich, N., Casino, P., Niks, D., Blumenstein, L., Barends, T. R., Kulik, V., Weyand, M., Schlichting, I., and Dunn, M. F. (2007) Biochemistry 46, 7713-7727].
+The line below this paragraph, {{ABSTRACT_PUBMED_17559232}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_17559232}}
 ==About this Structure==
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 [[Category: Pyridoxal phosphate]]
 [[Category: Tryptophan biosynthesis]]
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