1ci7

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{{STRUCTURE_1ci7| PDB=1ci7 | SCENE= }}
{{STRUCTURE_1ci7| PDB=1ci7 | SCENE= }}
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'''TERNARY COMPLEX OF THYMIDYLATE SYNTHASE FROM PNEUMOCYSTIS CARINII'''
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===TERNARY COMPLEX OF THYMIDYLATE SYNTHASE FROM PNEUMOCYSTIS CARINII===
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==Overview==
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Thymidylate synthase (TS), a half-the-sites reactive enzyme, catalyzes the final step in the de novo biosynthesis of deoxythymidine monophosphate, dTMP, required for DNA replication. The cocrystal structure of TS from Pneumocystis carinii (PcTS), a new drug target for an important pathogen, with its substrate, deoxyuridine monophosphate (dUMP), and a cofactor mimic, CB3717, was determined. The structure, solved at 2.6 A resolution, shows an asymmetric dimer with two molecules of the substrate dUMP bound yet only one molecule of cofactor analogue bound. The structural evidence reveals that upon binding cofactor analogue and forming a covalent bond from the nucleophilic cysteine to the substrate, dUMP, at one active site, PcTS undergoes a conformational change that renders the opposite monomer incapable of forming a covalent bond or binding a molecule of cofactor analogue. The communication pathway between the two active sites is evident, allowing a structural definition of the basis of half-the-sites reactivity for thymidylate synthase and providing an example of such a mechanism for other half-the-sites reactive enzymes.
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{{ABSTRACT_PUBMED_10529228}}
==About this Structure==
==About this Structure==
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[[Category: Methyltransferase]]
[[Category: Methyltransferase]]
[[Category: Nucleotide biosynthesis]]
[[Category: Nucleotide biosynthesis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:45:30 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:46:42 2008''

Revision as of 17:46, 30 June 2008

Image:1ci7.png

Template:STRUCTURE 1ci7

TERNARY COMPLEX OF THYMIDYLATE SYNTHASE FROM PNEUMOCYSTIS CARINII

Template:ABSTRACT PUBMED 10529228

About this Structure

1CI7 is a Single protein structure of sequence from Pneumocystis carinii. Full crystallographic information is available from OCA.

Reference

The structural mechanism for half-the-sites reactivity in an enzyme, thymidylate synthase, involves a relay of changes between subunits., Anderson AC, O'Neil RH, DeLano WL, Stroud RM, Biochemistry. 1999 Oct 19;38(42):13829-36. PMID:10529228

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