Asp-52 in Combination with Asp-398 Plays a Critical Role in ATP Hydrolysis of Chaperonin GroEL

The Escherichia coli chaperonin GroEL is a double-ring chaperone that assists protein folding with the aid of GroES and ATP. Asp-398 in GroEL is known as one of the critical residues on ATP hydrolysis because GroEL(D398A) mutant is deficient in ATP hydrolysis (

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Bibliographische Detailangaben
Veröffentlicht in:	The Journal of biological chemistry 2014-10, Vol.289 (43), p.30005-30011
Hauptverfasser:	Koike-Takeshita, Ayumi, Mitsuoka, Kaoru, Taguchi, Hideki
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Triphosphate - metabolism Aspartic Acid - metabolism Binding Sites Chaperonin 10 - metabolism Chaperonin 10 - ultrastructure Chaperonin 60 - chemistry Chaperonin 60 - metabolism Chaperonin 60 - ultrastructure Escherichia coli - metabolism Hydrolysis Malate Dehydrogenase - metabolism Mutant Proteins - metabolism Negative Staining Protein Folding Protein Stability Protein Structure and Folding Protein Subunits - chemistry Protein Subunits - metabolism Structure-Activity Relationship Thiosulfate Sulfurtransferase - metabolism
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Beschreibung
Zusammenfassung:	The Escherichia coli chaperonin GroEL is a double-ring chaperone that assists protein folding with the aid of GroES and ATP. Asp-398 in GroEL is known as one of the critical residues on ATP hydrolysis because GroEL(D398A) mutant is deficient in ATP hydrolysis (
ISSN:	0021-9258 1083-351X
DOI:	10.1074/jbc.M114.593822