Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 448-459 |
| Number of pages | 12 |
| Journal | Journal of Molecular Biology |
| Volume | 394 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - Dec 4 2009 |
| Externally published | Yes |
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All Science Journal Classification (ASJC) codes
- Molecular Biology
Cite this
Crystal Structure of HypA, a Nickel-Binding Metallochaperone for [NiFe] Hydrogenase Maturation. / Watanabe, Satoshi; Arai, Takayuki; Matsumi, Rie; Atomi, Haruyuki; Imanaka, Tadayuki; Miki, Kunio.
In: Journal of Molecular Biology, Vol. 394, No. 3, 04.12.2009, p. 448-459.Research output: Contribution to journal › Article
}
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
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.
UR - http://www.scopus.com/inward/record.url?scp=70350728386&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=70350728386&partnerID=8YFLogxK
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 -