N. Numoto

Publications67
h-index8
Citations265
Highly Influential Citations20
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Inter‐subunit interaction and quaternary rearrangement defined by the central stalk of prokaryotic V1‐ATPase
V‐type ATPases (V‐ATPases) are categorized as rotary ATP synthase/ATPase complexes. The V‐ATPases are distinct from F‐ATPases in terms of their rotation scheme, architecture and subunit composition.… Expand
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Structure of an extracellular giant hemoglobin of the gutless beard worm Oligobrachia mashikoi.
Mouthless and gutless marine animals, pogonophorans and vestimentiferans, obtain their nutrition solely from their symbiotic chemoautotrophic sulfur-oxidizing bacteria. These animals have… Expand
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Origin of asymmetry at the intersubunit interfaces of V1-ATPase from Thermus thermophilus.
V-type ATPase (V-ATPase) is one of the rotary ATPase complexes that mediate energy conversion between the chemical energy of ATP and the ion gradient across the membrane through a rotary catalytic… Expand
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Crystal structure of archaeal photolyase from Sulfolobus tokodaii with two FAD molecules: implication of a novel light-harvesting cofactor.
UV exposure of DNA molecules induces serious DNA lesions. The cyclobutane pyrimidine dimer (CPD) photolyase repairs CPD-type - lesions by using the energy of visible light. Two chromophores for… Expand
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Structure of the C subunit of V-type ATPase from Thermus thermophilus at 1.85 A resolution.
The V-type H(+)-ATPases are similar to the F-type ATP synthases in their structure and functional mechanism. They hydrolyze ATP coupled with proton translocation across a membrane, but in some… Expand
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Structural Dynamics of the PET-Degrading Cutinase-like Enzyme from Saccharomonospora viridis AHK190 in Substrate-Bound States Elucidates the Ca2+-Driven Catalytic Cycle
A cutinase-type polyesterase from Saccharomonospora viridis AHK190 (Cut190) has been shown to degrade the inner block of polyethylene terephthalate. A unique feature of Cut190 is that its function… Expand
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Crystal structure of the Co‐chaperonin Cpn10 from Thermus thermophilus HB8
Introduction. Chaperonins are ubiquitous proteins that control the folding of other proteins denatured by various stresses, such as heat shock. They consist of two types of proteins, cpn60 (60 kDa)… Expand
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Structure of the partially unliganded met state of 400 kDa hemoglobin: Insights into ligand‐induced structural changes of giant hemoglobins
Recent crystallographic studies have revealed the structures of some invertebrate extracellular giant hemoglobins of 3,600 kDa or 400 kDa and their common quaternary structure of dodecameric… Expand
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Structural basis for the heterotropic and homotropic interactions of invertebrate giant hemoglobin.
The oxygen binding properties of extracellular giant hemoglobins (Hbs) in some annelids exhibit features significantly different from those of vertebrate tetrameric Hbs. Annelid giant Hbs show… Expand
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Structural Dynamics of the PET-Degrading Cutinase-like Enzyme from Saccharomonospora viridis AHK190 in Substrate-Bound States Elucidates the Ca2+-Driven Catalytic Cycle.
A cutinase-type polyesterase from Saccharomonospora viridis AHK190 (Cut190) has been shown to degrade the inner block of polyethylene terephthalate. A unique feature of Cut190 is that its function… Expand
  • 9