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| | {{STRUCTURE_2bbq| PDB=2bbq | SCENE= }} | | {{STRUCTURE_2bbq| PDB=2bbq | SCENE= }} |
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| - | '''STRUCTURAL BASIS FOR RECOGNITION OF POLYGLUTAMYL FOLATES BY THYMIDYLATE SYNTHASE'''
| + | ===STRUCTURAL BASIS FOR RECOGNITION OF POLYGLUTAMYL FOLATES BY THYMIDYLATE SYNTHASE=== |
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| - | ==Overview==
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| - | Thymidylate synthase (TS) catalyzes the final step in the de novo synthesis of thymidine. In vivo TS binds a polyglutamyl cofactor, polyglutamyl methylenetetrahydrofolate (CH2-H4folate), which serves as a carbon donor. Glutamate residues on the cofactor contribute as much as 3.7 kcal to the interaction between the cofactor, substrate, and enzyme. Because many ligand/receptor interactions appear to be driven largely by hydrophobic forces, it is surprising that the addition of hydrophilic, soluble groups such as glutamates increases the affinity of the cofactor for TS. The structure of a polyglutamyl cofactor analog bound in ternary complex with deoxyuridine monophosphate (dUMP) and Escherichia coli TS reveals how the polyglutamyl moiety is positioned in TS and accounts in a qualitative way for the binding contributions of the different individual glutamate residues. The polyglutamyl moiety is not rigidly fixed by its interaction with the protein except for the first glutamate residue nearest the p-aminobenzoic acid ring of folate. Each additional glutamate is progressively more disordered than the previous one in the chain. The position of the second and third glutamate residues on the protein surface suggests that the polyglutamyl binding site could be utilized by a new family of inhibitors that might fill the binding area more effectively than polyglutamate.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_1390771}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 1390771 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_1390771}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Kamb, A.]] | | [[Category: Kamb, A.]] |
| | [[Category: Stroud, R M.]] | | [[Category: Stroud, R M.]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:04:57 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 05:33:03 2008'' |
Revision as of 02:33, 28 July 2008
Template:STRUCTURE 2bbq
STRUCTURAL BASIS FOR RECOGNITION OF POLYGLUTAMYL FOLATES BY THYMIDYLATE SYNTHASE
Template:ABSTRACT PUBMED 1390771
About this Structure
2BBQ is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structural basis for recognition of polyglutamyl folates by thymidylate synthase., Kamb A, Finer-Moore J, Calvert AH, Stroud RM, Biochemistry. 1992 Oct 20;31(41):9883-90. PMID:1390771
Page seeded by OCA on Mon Jul 28 05:33:03 2008
