Crystallization and preliminary characterization of the Thermus thermophilus RNA helicase Hera C-terminal domain.
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A novel dimerization motif in the C-terminal domain of the Thermus thermophilus DEAD box helicase Hera confers substantial flexibilityThe Thermus thermophilus DEAD box helicase Hera contains a modified RNA recognition motif domain loosely connected to the helicase coreRecognition of two distinct elements in the RNA substrate by the RNA-binding domain of the T. thermophilus DEAD box helicase HeraThe mechanism of ATP-dependent RNA unwinding by DEAD box proteins.DEAD-box RNA helicase domains exhibit a continuum between complete functional independence and high thermodynamic coupling in nucleotide and RNA duplex recognition.
P2860
Crystallization and preliminary characterization of the Thermus thermophilus RNA helicase Hera C-terminal domain.
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article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 14 February 2009
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Crystallization and preliminar ...... licase Hera C-terminal domain.
@en
Crystallization and preliminar ...... licase Hera C-terminal domain.
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type
label
Crystallization and preliminar ...... licase Hera C-terminal domain.
@en
Crystallization and preliminar ...... licase Hera C-terminal domain.
@nl
prefLabel
Crystallization and preliminar ...... licase Hera C-terminal domain.
@en
Crystallization and preliminar ...... licase Hera C-terminal domain.
@nl
P2093
P2860
P1476
Crystallization and preliminar ...... licase Hera C-terminal domain.
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P2093
Dagmar Klostermeier
Julia G Wittmann
Markus G Rudolph
P2860
P304
P356
10.1107/S1744309108043145
P577
2009-02-14T00:00:00Z