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PDBsum entry 1b02

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protein ligands links
Transferase PDB id
1b02
Jmol
Contents
Protein chain
279 a.a. *
Ligands
UFP-C2F
Waters ×84
* Residue conservation analysis
PDB id:
1b02
Name: Transferase
Title: Crystal structure of thymidylate synthase a from bacillus su
Structure: Protein (thymidylate synthase). Chain: a. Engineered: yes
Source: Bacillus subtilis. Organism_taxid: 1423. Strain: 168. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.50Å     R-factor:   0.194     R-free:   0.233
Authors: K.M.Fox,F.Maley,A.Garibian,L.Changchien,P.Vanroey
Key ref: K.M.Fox et al. (1999). Crystal structure of thymidylate synthase A from Bacillus subtilis. Protein Sci, 8, 538-544. PubMed id: 10091656 DOI: 10.1110/ps.8.3.538
Date:
16-Nov-98     Release date:   29-Mar-99    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P0CI79  (TYSY1_BACSU) -  Thymidylate synthase 1
Seq:
Struc:
279 a.a.
279 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.2.1.1.45  - Thymidylate synthase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
Folate Coenzymes
      Reaction: 5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP
5,10-methylenetetrahydrofolate
Bound ligand (Het Group name = C2F)
corresponds exactly
+
dUMP
Bound ligand (Het Group name = UFP)
matches with 95.24% similarity
= dihydrofolate
+ dTMP
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   1 term 
  Biological process     methylation   4 terms 
  Biochemical function     transferase activity     3 terms  

 

 
    reference    
 
 
DOI no: 10.1110/ps.8.3.538 Protein Sci 8:538-544 (1999)
PubMed id: 10091656  
 
 
Crystal structure of thymidylate synthase A from Bacillus subtilis.
K.M.Fox, F.Maley, A.Garibian, L.M.Changchien, P.Van Roey.
 
  ABSTRACT  
 
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.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
18275083 B.C.Lee, K.Park, and D.Kim (2008).
Analysis of the residue-residue coevolution network and the functionally important residues in proteins.
  Proteins, 72, 863-872.  
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