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1vzc

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{{STRUCTURE_1vzc| PDB=1vzc | SCENE= }}
{{STRUCTURE_1vzc| PDB=1vzc | SCENE= }}
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'''L. CASEI THYMIDYLATE SYNTHASE MUTANT E60Q BINARY COMPLEX WITH FDUMP'''
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===L. CASEI THYMIDYLATE SYNTHASE MUTANT E60Q BINARY COMPLEX WITH FDUMP===
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==Overview==
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Three steps along the pathway of binding, orientation of substrates and release of products are revealed by X-ray crystallographic structures of ternary complexes of the wild-type Lactobacillus casei thymidylate synthase enzyme. Each complex was formed by diffusion of either the cofactor 5,10-methylene-5,6,7,8-tetrahydrofolate or the folate analog 10-propargyl-5,8-dideazafolate into binary co-crystals of thymidylate synthase with 2'-deoxyuridine-5'-monophosphate. A two-substrate/enzyme complex is formed where the substrates remain unaltered. The imidazolidine ring is unopened and the pterin of the 5,10-methylene-5,6,7,8-tetrahydrofolate cofactor binds at an unproductive "alternate" site. We propose that the presence of the pterin at this site may represent an initial interaction with the enzyme that precedes all catalytic events. The structure of the 2'-deoxyuridine-5'-monophosphate and 10-propargyl-5,8-dideazafolate folate analog complex identifies both ligands in orientations favorable for the initiation of catalysis and resembles the productive complex. A product complex where the ligands have been converted into products of the thymidylate synthase reaction within the crystal, 2'-deoxythymidine-5'-monophosphate and 7,8-dihydrofolate, shows how ligands are situated within the enzyme after catalysis and on the way to product release.
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==About this Structure==
==About this Structure==
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[[Category: Methyltransferase]]
[[Category: Methyltransferase]]
[[Category: Nucleotide synthase]]
[[Category: Nucleotide synthase]]
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Revision as of 11:06, 27 July 2008

Image:1vzc.png

Template:STRUCTURE 1vzc

L. CASEI THYMIDYLATE SYNTHASE MUTANT E60Q BINARY COMPLEX WITH FDUMP

Template:ABSTRACT PUBMED 8568895

About this Structure

1VZC is a Single protein structure of sequence from Lactobacillus casei. Full crystallographic information is available from OCA.

Reference

Entropy in bi-substrate enzymes: proposed role of an alternate site in chaperoning substrate into, and products out of, thymidylate synthase., Birdsall DL, Finer-Moore J, Stroud RM, J Mol Biol. 1996 Jan 26;255(3):522-35. PMID:8568895

Page seeded by OCA on Sun Jul 27 14:05:52 2008

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