A Structural mechanism for dimeric to tetrameric oligomer conversion in sp. nucleoside diphosphate kinase

Arai, Shigeki; Yonezawa, Yasushi; Okazaki, Nobuo; Matsumoto, Fumiko; Tamada, Taro; Tokunaga, Hiroko*; Ishibashi, Matsujiro*; Blaber, M.; Tokunaga, Masao*; Kuroki, Ryota

In order to clarify the oligomer state of nucleoside diphosphate kinase (NDK) from moderately halophilic sp. 593 (HaNDK), the crystal structure of HaNDK was determined by X-ray crystallography. The crystal structures of the wild-type HaNDK and the mutant HaNDK (E134A) showed a dimer and a tetramer, respectively. The higher ordered association of proteins usually contributes to an increase in thermal stability and substrate affinity. The change in the assembly form by a minimum mutation may be an effective way for NDK to acquire molecular characteristics suited to various circumstances.

Language	:	English
Journal	:	Protein Science
Volume	:	21
Number	:	4
Pages	:	p.498 - 510
Publication Year/Month	:	2012/04
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Paper URL	:	https://doi.org/10.1002/pro.2032
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Keywords	:	no keyword
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Article of JAEA R&D Review	:	Developing a Technique for Operating a Protein Assembly; Identification of the Key Residue Controlling Protein Assembly via X-ray Crystallography[/]
Cooperating Institute	:	鹿児島大学

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Registration No. : AA20111013
JAEA Abstracts No. : 40000977
Paper Submission No. : 10998

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