1b02

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[[Image:1b02.gif|left|200px]]
[[Image:1b02.gif|left|200px]]
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{{Structure
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|PDB= 1b02 |SIZE=350|CAPTION= <scene name='initialview01'>1b02</scene>, resolution 2.5&Aring;
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The line below this paragraph, containing "STRUCTURE_1b02", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=C2F:5-METHYL-5,6,7,8-TETRAHYDROFOLIC+ACID'>C2F</scene>, <scene name='pdbligand=UFP:5-FLUORO-2&#39;-DEOXYURIDINE-5&#39;-MONOPHOSPHATE'>UFP</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1b02| PDB=1b02 | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1b02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b02 OCA], [http://www.ebi.ac.uk/pdbsum/1b02 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1b02 RCSB]</span>
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}}
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'''CRYSTAL STRUCTURE OF THYMIDYLATE SYNTHASE A FROM BACILLUS SUBTILIS'''
'''CRYSTAL STRUCTURE OF THYMIDYLATE SYNTHASE A FROM BACILLUS SUBTILIS'''
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[[Category: Maley, F.]]
[[Category: Maley, F.]]
[[Category: Vanroey, P.]]
[[Category: Vanroey, P.]]
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[[Category: methyltransferase]]
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[[Category: Methyltransferase]]
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[[Category: transferase]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:54:04 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:50:53 2008''
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Revision as of 07:54, 2 May 2008

Image:1b02.gif

Template:STRUCTURE 1b02

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 Page seeded by OCA on Fri May 2 10:54:04 2008

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