1ci7: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
Line 1: Line 1:
[[Image:1ci7.jpg|left|200px]]
{{Seed}}
[[Image:1ci7.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ci7|  PDB=1ci7  |  SCENE=  }}  
{{STRUCTURE_1ci7|  PDB=1ci7  |  SCENE=  }}  


'''TERNARY COMPLEX OF THYMIDYLATE SYNTHASE FROM PNEUMOCYSTIS CARINII'''
===TERNARY COMPLEX OF THYMIDYLATE SYNTHASE FROM PNEUMOCYSTIS CARINII===




==Overview==
<!--
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.
The line below this paragraph, {{ABSTRACT_PUBMED_10529228}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 10529228 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_10529228}}


==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Methyltransferase]]
[[Category: Methyltransferase]]
[[Category: Nucleotide biosynthesis]]
[[Category: Nucleotide biosynthesis]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 12:45:30 2008''
 
''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

File: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

Page seeded by OCA on Mon Jun 30 20:46:42 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1ci7&oldid=582729"