TY - JOUR
T1 - Crystal structure of family 4 uracil-DNA glycosylase from Sulfolobus tokodaii and a function of tyrosine 170 in DNA binding
AU - Kawai, Akito
AU - Higuchi, Shigesada
AU - Tsunoda, Masaru
AU - Nakamura, Kazuo T.
AU - Yamagata, Yuriko
AU - Miyamoto, Shuichi
N1 - Funding Information:
We are grateful to Dr. Masato Yoshimura, Dr. Eiki Yamashita, Professor Atsushi Nakagawa, and the beamline staff for their support at the BL44XU in the SPring-8. Synchrotron experiments were performed with the approval of the Joint Research Committee of the Institute for Protein Research, Osaka University, and the Japan Synchrotron Radiation Research Institute (Proposal No. 2007B6927). This work was partly supported by the National Project on Protein Structural and Functional Analysis by the Ministry of Education, Culture, Sports, Science and Technology of Japan (Protein 3000 project). This work was also partly supported by KUMAYAKU Alumni Research Fund .
Publisher Copyright:
© 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
PY - 2015/9/14
Y1 - 2015/9/14
N2 - Uracil-DNA glycosylases (UDGs) excise uracil from DNA by catalyzing the N-glycosidic bond hydrolysis. Here we report the first crystal structures of an archaeal UDG (stoUDG). Compared with other UDGs, stoUDG has a different structure of the leucine-intercalation loop, which is important for DNA binding. The stoUDG-DNA complex model indicated that Leu169, Tyr170, and Asn171 in the loop are involved in DNA intercalation. Mutational analysis showed that Tyr170 is critical for substrate DNA recognition. These results indicate that Tyr170 occupies the intercalation site formed after the structural change of the leucine-intercalation loop required for the catalysis.
AB - Uracil-DNA glycosylases (UDGs) excise uracil from DNA by catalyzing the N-glycosidic bond hydrolysis. Here we report the first crystal structures of an archaeal UDG (stoUDG). Compared with other UDGs, stoUDG has a different structure of the leucine-intercalation loop, which is important for DNA binding. The stoUDG-DNA complex model indicated that Leu169, Tyr170, and Asn171 in the loop are involved in DNA intercalation. Mutational analysis showed that Tyr170 is critical for substrate DNA recognition. These results indicate that Tyr170 occupies the intercalation site formed after the structural change of the leucine-intercalation loop required for the catalysis.
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U2 - 10.1016/j.febslet.2015.08.019
DO - 10.1016/j.febslet.2015.08.019
M3 - Article
C2 - 26318717
AN - SCOPUS:84941424421
VL - 589
SP - 2675
EP - 2682
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 19
ER -