1O26
Crystal structure of Thymidylate Synthase Complementing Protein (TM0449) from Thermotoga maritima with FAD and dUMP at 1.6 A resolution
Summary for 1O26
Entry DOI | 10.2210/pdb1o26/pdb |
Related | 1O24 1O25 1O27 1O28 1O29 1O2A 1O2B |
Descriptor | Thymidylate synthase thyX, 2'-DEOXYURIDINE 5'-MONOPHOSPHATE, FLAVIN-ADENINE DINUCLEOTIDE, ... (5 entities in total) |
Functional Keywords | tm0449, thymidylate synthase complementing protein, structural genomics, jcsg, psi, joint center for structural genomics, protein structure initiative, transferase |
Biological source | Thermotoga maritima |
Total number of polymer chains | 4 |
Total formula weight | 115140.51 |
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 Cited by 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: 12791256DOI: 10.1016/S0969-2126(03)00097-2 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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