Literature summary for 2.3.1.B43 extracted from

Zhao, K.; Chai, X.; Marmorstein, R.
Structure and substrate binding properties of cobB, a Sir2 homolog protein deacetylase from Escherichia coli (2004), J. Mol. Biol., 337, 731-741.

Search for more literature for 2.3.1.B43

Cloned(Commentary)

Cloned (Comment)	Organism
overexpression in Escherichia coli BL21	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystals of native and selenomethionine-derivatized cobB are grown at room temperature using the hanging-drop, vapor-diffusion method. The crystal structure of the Escherichia coli cobB core domain (residues 40274) in complex with an 11-residue peptide containing residues 1219 of histone H4 and acetylated at lysine 16 is determined by a combination of Zn2+ and Se multiwavelength anomalous diffraction to 1.96 A resolution	Escherichia coli

Crystallization (Comment)

Organism

crystals of native and selenomethionine-derivatized cobB are grown at room temperature using the hanging-drop, vapor-diffusion method. The crystal structure of the Escherichia coli cobB core domain (residues 40274) in complex with an 11-residue peptide containing residues 1219 of histone H4 and acetylated at lysine 16 is determined by a combination of Zn2+ and Se multiwavelength anomalous diffraction to 1.96 A resolution

Escherichia coli

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Zn2+	the zinc-binding domain of the sirtuin proteins may play a similar role in substrate-specific recognition	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P75960	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Escherichia coli

Synonyms

Synonyms	Comment	Organism
CobB	-	Escherichia coli

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Release 2023.1 (January 2023)