1b02
From Proteopedia
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| - | [[Image:1b02.gif|left|200px]] | + | [[Image:1b02.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF THYMIDYLATE SYNTHASE A FROM BACILLUS SUBTILIS''' | + | {{Structure |
| + | |PDB= 1b02 |SIZE=350|CAPTION= <scene name='initialview01'>1b02</scene>, resolution 2.5Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=UFP:5-FLUORO-2'-DEOXYURIDINE-5'-MONOPHOSPHATE'>UFP</scene> and <scene name='pdbligand=C2F:5-METHYL-5,6,7,8-TETRAHYDROFOLIC ACID'>C2F</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= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF THYMIDYLATE SYNTHASE A FROM BACILLUS SUBTILIS''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1B02 is a [ | + | 1B02 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B02 OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of thymidylate synthase A from Bacillus subtilis., Fox KM, Maley F, Garibian A, Changchien LM, Van Roey P, Protein Sci. 1999 Mar;8(3):538-44. PMID:[http:// | + | Crystal structure of thymidylate synthase A from Bacillus subtilis., Fox KM, Maley F, Garibian A, Changchien LM, Van Roey P, Protein Sci. 1999 Mar;8(3):538-44. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10091656 10091656] |
[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[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 10:04:30 2008'' |
Revision as of 08:04, 20 March 2008
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| , resolution 2.5Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Activity: | Thymidylate synthase, with EC number 2.1.1.45 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THYMIDYLATE SYNTHASE A FROM BACILLUS SUBTILIS
Overview
Thymidylate synthase (TS) converts dUMP to dTMP by reductive methylation, where 5,10-methylenetetrahydrofolate is the source of both the methylene group and reducing equivalents. The mechanism of this reaction has been extensively studied, mainly using the enzyme from Escherichia coli. Bacillus subtilis contains two genes for TSs, ThyA and ThyB. The ThyB enzyme is very similar to other bacterial TSs, but the ThyA enzyme is quite different, both in sequence and activity. In ThyA TS, the active site histidine is replaced by valine. In addition, the B. subtilis enzyme has a 2.4-fold greater k(cat) than the E. coli enzyme. The structure of B. subtilis thymidylate synthase in a ternary complex with 5-fluoro-dUMP and 5,10-methylenetetrahydrofolate has been determined to 2.5 A resolution. Overall, the structure of B. subtilis TS (ThyA) is similar to that of the E. coli enzyme. However, there are significant differences in the structures of two loops, the dimer interface and the details of the active site. The effects of the replacement of histidine by valine and a serine to glutamine substitution in the active site area, and the addition of a loop over the carboxy terminus may account for the differences in k(cat) found between the two enzymes.
About this Structure
1B02 is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
Crystal structure of thymidylate synthase A from Bacillus subtilis., Fox KM, Maley F, Garibian A, Changchien LM, Van Roey P, Protein Sci. 1999 Mar;8(3):538-44. PMID:10091656
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