1ci7: Difference between revisions
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[[Image:1ci7.jpg|left|200px]] | [[Image:1ci7.jpg|left|200px]] | ||
'''TERNARY COMPLEX OF THYMIDYLATE SYNTHASE FROM PNEUMOCYSTIS CARINII''' | {{Structure | ||
|PDB= 1ci7 |SIZE=350|CAPTION= <scene name='initialview01'>1ci7</scene>, resolution 2.6Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=UMP:2'-DEOXYURIDINE+5'-MONOPHOSPHATE'>UMP</scene> and <scene name='pdbligand=CB3:10-PROPARGYL-5,8-DIDEAZAFOLIC ACID'>CB3</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Thymidylate_synthase Thymidylate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.45 2.1.1.45] | |||
|GENE= | |||
}} | |||
'''TERNARY COMPLEX OF THYMIDYLATE SYNTHASE FROM PNEUMOCYSTIS CARINII''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1CI7 is a [ | 1CI7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pneumocystis_carinii Pneumocystis carinii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CI7 OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10529228 10529228] | ||
[[Category: Pneumocystis carinii]] | [[Category: Pneumocystis carinii]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: nucleotide biosynthesis]] | [[Category: nucleotide biosynthesis]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:24:41 2008'' | ||
Revision as of 11:24, 20 March 2008
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| , resolution 2.6Å | |||||||
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| Ligands: | and | ||||||
| Activity: | Thymidylate synthase, with EC number 2.1.1.45 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
TERNARY COMPLEX OF THYMIDYLATE SYNTHASE FROM PNEUMOCYSTIS CARINII
OverviewOverview
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.
About this StructureAbout this Structure
1CI7 is a Single protein structure of sequence from Pneumocystis carinii. Full crystallographic information is available from OCA.
ReferenceReference
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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