4A35
Crystal structure of human Mitochondrial enolase superfamily member 1 (ENOSF1)
Summary for 4A35
| Entry DOI | 10.2210/pdb4a35/pdb |
| Descriptor | MITOCHONDRIAL ENOLASE SUPERFAMILY MEMBER 1, MAGNESIUM ION, 1,2-ETHANEDIOL, ... (4 entities in total) |
| Functional Keywords | isomerase |
| Biological source | HOMO SAPIENS (HUMAN) |
| Total number of polymer chains | 1 |
| Total formula weight | 50050.23 |
| Authors | Muniz, J.R.C.,Froese, D.S.,Krojer, T.,Vollmar, M.,Canning, P.,von Delft, F.,Arrowsmith, C.H.,Edwards, A.M.,Weigelt, J.,Bountra, C.,Oppermann, U.,Yue, W.W. (deposition date: 2011-09-30, release date: 2011-10-12, Last modification date: 2024-05-08) |
| Primary citation | Wichelecki, D.J.,Froese, D.S.,Kopec, J.,Muniz, J.R.,Yue, W.W.,Gerlt, J.A. Enzymatic and structural characterization of rTS gamma provides insights into the function of rTS beta. Biochemistry, 53:2732-2738, 2014 Cited by PubMed Abstract: In humans, the gene encoding a reverse thymidylate synthase (rTS) is transcribed in the reverse direction of the gene encoding thymidylate synthase (TS) that is involved in DNA biosynthesis. Three isoforms are found: α, β, and γ, with the transcript of the α-isoform overlapping with that of TS. rTSβ has been of interest since the discovery of its overexpression in methotrexate and 5-fluorouracil resistant cell lines. Despite more than 20 years of study, none of the rTS isoforms have been biochemically or structurally characterized. In this study, we identified rTSγ as an l-fuconate dehydratase and determined its high-resolution crystal structure. Our data provide an explanation for the observed difference in enzymatic activities between rTSβ and rTSγ, enabling more informed proposals for the possible function of rTSβ in chemotherapeutic resistance. PubMed: 24697329DOI: 10.1021/bi500349e PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.74 Å) |
Structure validation
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