1bq2
From Proteopedia
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| - | [[Image:1bq2.gif|left|200px]] | + | [[Image:1bq2.gif|left|200px]] |
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| - | '''E. COLI THYMIDYLATE SYNTHASE MUTANT N177A''' | + | {{Structure |
| + | |PDB= 1bq2 |SIZE=350|CAPTION= <scene name='initialview01'>1bq2</scene>, resolution 2.20Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=PO4:PHOSPHATE ION'>PO4</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= THYA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | }} | ||
| + | |||
| + | '''E. COLI THYMIDYLATE SYNTHASE MUTANT N177A''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1BQ2 is a [ | + | 1BQ2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BQ2 OCA]. |
==Reference== | ==Reference== | ||
| - | Inactivity of N229A thymidylate synthase due to water-mediated effects: isolating a late stage in methyl transfer., Reyes CL, Sage CR, Rutenber EE, Nissen RM, Finer-Moore JS, Stroud RM, J Mol Biol. 1998 Dec 4;284(3):699-712. PMID:[http:// | + | Inactivity of N229A thymidylate synthase due to water-mediated effects: isolating a late stage in methyl transfer., Reyes CL, Sage CR, Rutenber EE, Nissen RM, Finer-Moore JS, Stroud RM, J Mol Biol. 1998 Dec 4;284(3):699-712. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9826509 9826509] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: PO4]] | [[Category: PO4]] | ||
[[Category: methyltransferase]] | [[Category: methyltransferase]] | ||
| - | [[Category: substrate | + | [[Category: substrate module]] |
[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''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 10:14:15 2008'' |
Revision as of 08:14, 20 March 2008
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| , resolution 2.20Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | THYA (Escherichia coli) | ||||||
| Activity: | Thymidylate synthase, with EC number 2.1.1.45 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
E. COLI THYMIDYLATE SYNTHASE MUTANT N177A
Overview
Mutation of thymidylate synthase N229(177) to alanine results in an essentially inactive enzyme, yet it leads to formation of a stable ternary complex. The kinetics of N229(177)A show that kcat for Escherichia coli is reduced by 200-fold while the Km for dUMP is increased 200-fold and the Km for folate increased by tenfold versus the wild-type enzyme. The crystal structures of N229(177)A in complex with dUMP and CB3717, and in complex with dUMP alone are determined at 2.4 A, and 2.5 A resolution. These structures identify the covalently bound ternary complex and show how N229(177)A traps an intermediate, and so becomes inactive in a later step of the reaction. Since the smaller alanine side-chain at N229(177)A does not directly sterically impair binding of ligands, the structures implicate, and place quantitative limits on the involvement of the structured water network in the active site of thymidylate synthase in both catalysis and in determining the binding affinity for dUMP (in contrast, the N229(177)V mutation in Lactobacillus casei has minimal effect on activity).
About this Structure
1BQ2 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Inactivity of N229A thymidylate synthase due to water-mediated effects: isolating a late stage in methyl transfer., Reyes CL, Sage CR, Rutenber EE, Nissen RM, Finer-Moore JS, Stroud RM, J Mol Biol. 1998 Dec 4;284(3):699-712. PMID:9826509
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