TY - JOUR
T1 - Crystal Structure of HypA, a Nickel-Binding Metallochaperone for [NiFe] Hydrogenase Maturation
AU - Watanabe, Satoshi
AU - Arai, Takayuki
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. This work was supported by 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, by Grants-in-Aid for Creative Scientific Research (18GS0421 to T.I.) and for Scientific Research (A) (20247009 to K.M.) from the Japan Society for the Promotion of Science, and by a grant from the Japan Foundation for Applied Enzymology (to K.M).
PY - 2009/12/4
Y1 - 2009/12/4
N2 - HypA is one of the auxiliary proteins involved in the maturation of [NiFe] hydrogenases. By an unknown mechanism, HypA functions as a metallochaperone in the insertion of the Ni atom into hydrogenases. We have determined the crystal structures of HypA from Thermococcus kodakaraensis KOD1 in both monomeric and dimeric states. The structure of the HypA monomer consists of Ni- and Zn-binding domains. The relative arrangement of the two metal-binding domains has been shown to be associated with local conformations of the conserved Ni-binding motif, suggesting a communication between the Ni- and Zn-binding sites. The HypA dimer has been shown to be stabilized by unexpected domain swapping through archaea-specific linker helices. In addition, the hexameric structure of HypA is formed in the crystal packing. Several hydrogen bonds and hydrophobic interactions stabilize the hexamer interface. These findings suggest the functional diversity of HypA proteins.
AB - HypA is one of the auxiliary proteins involved in the maturation of [NiFe] hydrogenases. By an unknown mechanism, HypA functions as a metallochaperone in the insertion of the Ni atom into hydrogenases. We have determined the crystal structures of HypA from Thermococcus kodakaraensis KOD1 in both monomeric and dimeric states. The structure of the HypA monomer consists of Ni- and Zn-binding domains. The relative arrangement of the two metal-binding domains has been shown to be associated with local conformations of the conserved Ni-binding motif, suggesting a communication between the Ni- and Zn-binding sites. The HypA dimer has been shown to be stabilized by unexpected domain swapping through archaea-specific linker helices. In addition, the hexameric structure of HypA is formed in the crystal packing. Several hydrogen bonds and hydrophobic interactions stabilize the hexamer interface. These findings suggest the functional diversity of HypA proteins.
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U2 - 10.1016/j.jmb.2009.09.030
DO - 10.1016/j.jmb.2009.09.030
M3 - Article
C2 - 19769985
AN - SCOPUS:70350728386
VL - 394
SP - 448
EP - 459
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
SN - 0022-2836
IS - 3
ER -