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Crystal Structure of the Protease Domain of a Heat-shock Protein HtrA from Thermotoga maritima *
The results suggest that the activation of the proteolytic function of HtrA at elevated temperatures might occur by a conformational change, which includes the opening of the helical lid to expose the active site and subsequent rearrangement of a catalytic triad and an oxyanion hole. Expand
1‐Di­methyl­amino‐3‐di­methyl­imino‐1‐phenyl­prop‐1‐ene perchlorate
The title compound, C13H19N2+·ClO4−, a 1-aryl­ated vinamidinium salt, has been found to crystallize in monoclinic space group P21/n at room temperature. The dihedral angle between the planarExpand
A poxvirus protein forms a complex with left-handed Z-DNA: crystal structure of a Yatapoxvirus Zalpha bound to DNA.
  • S. Ha, N. Lokanath, +5 authors K. Kim
  • Biology, Medicine
  • Proceedings of the National Academy of Sciences…
  • 5 October 2004
The crystal structure of the Zalpha domain is described from the E3L-like protein of Yaba-like disease virus, a Yatapoxvirus, in a complex with Z-DNA, solved at a 2.0-A resolution. Expand
Dimeric core structure of modular stator subunit E of archaeal H+ -ATPase.
The first crystal structure of subunit E of A-ATPase from Pyrococcus horikoshii OT3 is reported, which represents a novel fold and is suggested that both cytoplasm and membrane sides of the EH complex may interact with other subunits to link A(1) and A(0) parts. Expand
Crystal structures of native and xylosaccharide‐bound alkali thermostable xylanase from an alkalophilic Bacillus sp. NG‐27: Structural insights into alkalophilicity and implications for adaptation to
Comparison of the structure of BSX with those of other thermostable GH10 xylanases optimally active at acidic or close to neutral pH showed that the solvent‐exposed acidic amino acids, Asp and Glu, are markedly enhanced in BSX, while solvent-exposed Asn was noticeably depleted, suggesting that a protein surface rich in acidic residues may be an important feature common to these alkalophilic enzymes. Expand
Structure of aldolase from Thermus thermophilus HB8 showing the contribution of oligomeric state to thermostability.
It is concluded that the oligomeric state of 2-deoxyribose-5-phosphate aldolase is important for the thermostability and not for the catalytic function. Expand
Structural insights into the molecular mechanism of Escherichia coli SdiA, a quorum-sensing receptor.
  • T. Kim, T. Duong, +7 authors K. Kim
  • Chemistry, Medicine
  • Acta crystallographica. Section D, Biological…
  • 1 March 2014
It was confirmed that the binding affinity of SdiA for the uvrY promoter was reduced under oxidizing conditions, which suggested the possibility of regulation of S diA by multiple independent signals such as quorum-sensing inducers and the oxidation state of the cell. Expand
Structural basis for the reaction mechanism of UDP-glucose pyrophosphorylase
Isothermal titration calorimetry analyses demonstrated that Mg2+ ion plays a key role in the enzymatic activity of UGPase by enhancing the binding of U GPase to UTP or UDP-glucose, suggesting that this reaction is catalyzed by an ordered sequential Bi Bi mechanism. Expand
Structures of dimeric nonstandard nucleotide triphosphate pyrophosphatase from Pyrococcus horikoshii OT3: functional significance of interprotomer conformational changes.
A conformational analysis of the five snapshots of PhNTPase structures using the multiple superposition method reveals that IMP, ITP and Mn(2+) bind to the active site without inducing large local conformational changes, indicating that a combination of interdomain and interprotomer rigid-body shifts mainly describes the conformational change of PhnTPase. Expand
Molecular Crystals and Liquid Crystals
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