3ZR1

Crystal structure of human MTH1

Summary for 3ZR1

• Entry DOI: 10.2210/pdb3zr1/pdb
• Related: 1IRY 3ZR0
• Descriptor: 7,8-DIHYDRO-8-OXOGUANINE TRIPHOSPHATASE, ACETATE ION, SULFATE ION, ... (4 entities in total)
• Functional Keywords: hydrolase
• Biological source: HOMO SAPIENS (HUMAN)
• Total number of polymer chains: 2
• Total formula weight: 36445.26

Authors

Svensson, L.M.,Jemth, A.,Desroses, M.,Loseva, O.,Helleday, T.,Hogbom, M.,Stenmark, P. (deposition date: 2011-06-13, release date: 2011-07-27, Last modification date: 2023-12-20)

Primary citation

Svensson, L.M.,Jemth, A.,Desroses, M.,Loseva, O.,Helleday, T.,Hogbom, M.,Stenmark, P.
Crystal Structure of Human Mth1 and the 8-Oxo-Dgmp Product Complex.
FEBS Lett., 585:2617-, 2011

PubMed Abstract: MTH1 hydrolyzes oxidized nucleotide triphosphates, thereby preventing them from being incorporated into DNA. We here present the structures of human MTH1 (1.9Å) and its complex with the product 8-oxo-dGMP (1.8Å). Unexpectedly MTH1 binds the nucleotide in the anti conformation with no direct interaction between the 8-oxo group and the protein. We suggest that the specificity depends on the stabilization of an enol tautomer of the 8-oxo form of dGTP. The binding of the product induces no major structural changes. The structures reveal the mode of nucleotide binding in MTH1 and provide the structural basis for inhibitor design.

PubMed: 21787772
DOI: 10.1016/J.FEBSLET.2011.07.017

Experimental method

X-RAY DIFFRACTION (1.9 Å)