Structural highlights
Function
[HYPA_THEKO] Probably plays a role in a hydrogenase nickel cofactor insertion step (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Crystal structure of HypA, a nickel-binding metallochaperone for [NiFe] hydrogenase maturation.,Watanabe S, Arai T, Matsumi R, Atomi H, Imanaka T, Miki K J Mol Biol. 2009 Dec 4;394(3):448-59. Epub 2009 Sep 19. PMID:19769985[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Watanabe S, Arai T, Matsumi R, Atomi H, Imanaka T, Miki K. Crystal structure of HypA, a nickel-binding metallochaperone for [NiFe] hydrogenase maturation. J Mol Biol. 2009 Dec 4;394(3):448-59. Epub 2009 Sep 19. PMID:19769985 doi:10.1016/j.jmb.2009.09.030
