1O2A

Crystal structure of Thymidylate Synthase Complementing Protein (TM0449) from Thermotoga maritima with FAD at 1.8 A resolution

Summary for 1O2A

• Entry DOI: 10.2210/pdb1o2a/pdb
• Descriptor: Thymidylate synthase thyX, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total)
• Functional Keywords: tm0449, thymidylate synthase complementing protein, structural genomics, jcsg, joint center for structural genomics, psi, protein structure initiative, transferase
• Biological source: Thermotoga maritima
• Total number of polymer chains: 4
• Total formula weight: 113156.92

Authors

Mathews, I.I.,Deacon, A.M.,Canaves, J.M.,McMullan, D.,Lesley, S.A.,Agarwalla, S.,Kuhn, P.,Joint Center for Structural Genomics (JCSG) (deposition date: 2003-02-18, release date: 2003-06-24, Last modification date: 2023-09-20)

Primary citation

Mathews, I.I.,Deacon, A.M.,Canaves, J.M.,McMullan, D.,Lesley, S.A.,Agarwalla, S.,Kuhn, P.
Functional Analysis of Substrate and Cofactor Complex Structures of a Thymidylate Synthase-Complementing Protein
Structure, 11:677-690, 2003

PubMed Abstract: 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.

PubMed: 12791256
DOI: 10.1016/S0969-2126(03)00097-2

Experimental method

X-RAY DIFFRACTION (1.8 Å)