1O2A: Crystal Structure Of Thymidylate Synthase Complementing Protein (tm0449) From Thermotoga Maritima With Fad At 1.8 A Resolution

Like thymidylate synthase (TS) in eukaryotes, the thymidylate synthase-complementing proteins (TSCPs) are mandatory for cell survival of many prokaryotes in the absence of external sources of thymidylate. Details of the mechanism of this novel family of enzymes are unknown. Here, we report the structural and functional analysis of a TSCP from Thermotoga maritima and its complexes with substrate, analogs, and cofactor. The structures presented here provide a basis for rationalizing the TSCP catalysis and reveal the possibility of the design of an inhibitor. We have identified a new helix-loop-strand FAD binding motif characteristic of the enzymes in the TSCP family. The presence of a hydrophobic core with residues conserved among the TSCP family suggests a common overall fold.
PDB ID: 1O2ADownload
MMDB ID: 23508
PDB Deposition Date: 2003/2/18
Updated in MMDB: 2006/12
Experimental Method:
x-ray diffraction
Resolution: 1.8  Å
Source Organism:
Similar Structures:
Biological Unit for 1O2A: tetrameric; determined by author and by software (PISA)
Molecular Components in 1O2A
Label Count Molecule
Proteins (4 molecules)
Thymidylate Synthase Thyx(Gene symbol: thyX)
Molecule annotation
Chemicals (4 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB