Structure of the JmjC domain-containing protein NO66 complexed with ribosomal protein Rpl8

Wang, C.; Zhang, Q.; Hang, T.; Tao, Y.; Ma, X.; Wu, M.; Zhang, X.; Zang, J.

doi:10.1107/S1399004715012948

Acta Crystallographica Section D
Acta Crystallographica
Section D BIOLOGICAL CRYSTALLOGRAPHY

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Figure 5
Conformational changes of NO66 are induced by substrate binding. (a) A comparison of the complex structure of NO66^176–C–Rpl8^204–224 (orange) with NO66^176–C–Ni²⁺ (magenta) is shown. The enlarged view shows the conformational changes in the active site. The three β-sheets βX (271–274), βY (262–268) and βZ (404–408) and several loops are rearranged upon substrate binding. (b) Surface representation of NO66^176–C–Ni²⁺ (left) and the complex between NO66^176–C and Rpl8^204–224 (right) are shown. The distances between the active sites of NO66 in the two types of dimers are indicated. (c) A comparison of the structure of M2 (cyan) with one dimer of wild-type NO66 associated by interface I (magenta) is shown.

BIOLOGICAL
CRYSTALLOGRAPHY

ISSN: 1399-0047

Volume 71| Part 9| August 2015| Pages 1955-1964

doi:10.1107/S1399004715012948

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