TY - JOUR
T1 - Crystal structures of the HypCD complex and the HypCDE ternary complex
T2 - Transient intermediate complexes during [NiFe] hydrogenase maturation
AU - Watanabe, Satoshi
AU - Matsumi, Rie
AU - Atomi, Haruyuki
AU - Imanaka, Tadayuki
AU - Miki, Kunio
N1 - Funding Information:
We thank beamline scientists of SPring-8 and the Photon Factory for their help with X-ray data collection, S. Fujishima and I. Hamachi for assistance with the ITC experiments, T. Kanai and T. Sato for assistance with the anaerobic experiments, and M. Fujihashi and N. Numoto for reading the manuscript. This work was supported by Grants-in-Aid for Scientific Research (A) (20247009 and 23247014 to K.M.) and Creative Scientific Research (18GS0421 to T.I.) from the Japan Society for the Promotion of Science, a grant from the National Project on Protein Structural and Functional Analysis (to K.M. and T.I.) from the Ministry of Education, Culture, Sports, Science and Technology, Japan, and a grant from the Japan Foundation for Applied Enzymology (to K.M.).
PY - 2012/12/5
Y1 - 2012/12/5
N2 - [NiFe] hydrogenase maturation represents one of the most dynamic and sophisticated processes in metallocenter assembly. The Fe(CN)2CO moiety of [NiFe] hydrogenases is assembled via unknown transient interactions among specific maturation proteins HypC (metallochaperone), HypD (redox protein), and HypE (cyanide synthesis/donor). Here, we report the structures of the HypC-HypD and HypC-HypD-HypE complexes, providing a view of the transient interactions that take place during the maturation process. HypC binds to the conserved region of HypD through extensive hydrophobic interactions. The ternary complex formation between HypE and the HypCD complex involves both HypC and HypD, rendering the HypE conformation favorable for cyanide transfer. In the complex, the conserved cysteines of HypC and HypD form an Fe binding site. The conserved C-terminal cysteine of HypE can access the thiol redox cascade of HypD. These results provide structural insights into the Fe atom cyanation in the HypCDE complex.
AB - [NiFe] hydrogenase maturation represents one of the most dynamic and sophisticated processes in metallocenter assembly. The Fe(CN)2CO moiety of [NiFe] hydrogenases is assembled via unknown transient interactions among specific maturation proteins HypC (metallochaperone), HypD (redox protein), and HypE (cyanide synthesis/donor). Here, we report the structures of the HypC-HypD and HypC-HypD-HypE complexes, providing a view of the transient interactions that take place during the maturation process. HypC binds to the conserved region of HypD through extensive hydrophobic interactions. The ternary complex formation between HypE and the HypCD complex involves both HypC and HypD, rendering the HypE conformation favorable for cyanide transfer. In the complex, the conserved cysteines of HypC and HypD form an Fe binding site. The conserved C-terminal cysteine of HypE can access the thiol redox cascade of HypD. These results provide structural insights into the Fe atom cyanation in the HypCDE complex.
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U2 - 10.1016/j.str.2012.09.018
DO - 10.1016/j.str.2012.09.018
M3 - Article
C2 - 23123111
AN - SCOPUS:84870548822
VL - 20
SP - 2124
EP - 2137
JO - Structure with Folding & design
JF - Structure with Folding & design
SN - 0969-2126
IS - 12
ER -