Literature summary for 2.8.3.21 extracted from

Rangarajan, E.S.; Li, Y.; Iannuzzi, P.; Cygler, M.; Matte, A.
Crystal structure of Escherichia coli crotonobetainyl-CoA: carnitine CoA-transferase (CaiB) and its complexes with CoA and carnitinyl-CoA (2005), Biochemistry, 44, 5728-5738.

Cloned(Commentary)

Cloned (Comment)	Organism
-	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structures of apo-CaiB, as well as its Asp169Ala mutant bound to CoA and to carnitinyl-CoA, to 1.6, 2.4, and 2.4 A resolution, respectively. CaiB is composed of two identical circular chains that together form an intertwined dimer. Each monomer consists of a large domain, containing a Rossmann fold, and a small domain. The CoA cofactor-binding site is formed at the interface of the large domain of one monomer and the small domain from the second monomer. Most of the protein-CoA interactions are formed with the Rossmann fold domain. CoA binding results in a change in the relative positions of the large and small domains compared with apo-CaiB	Escherichia coli

Crystallization (Comment)

Organism

crystal structures of apo-CaiB, as well as its Asp169Ala mutant bound to CoA and to carnitinyl-CoA, to 1.6, 2.4, and 2.4 A resolution, respectively. CaiB is composed of two identical circular chains that together form an intertwined dimer. Each monomer consists of a large domain, containing a Rossmann fold, and a small domain. The CoA cofactor-binding site is formed at the interface of the large domain of one monomer and the small domain from the second monomer. Most of the protein-CoA interactions are formed with the Rossmann fold domain. CoA binding results in a change in the relative positions of the large and small domains compared with apo-CaiB

Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
D169A	utation of the predicted key catalytic residue. Upon cocrystallization with crotonoyl-CoA, electron density is observed only for the CoA region of the cofactor, ending at the sulfur atom as for the wild-type enzyme. When both carnitine and crotonoyl-CoA are cocrystallized with the mutant enzyme, the electron density observed in the binding site is consistent with formation of the product, carnitinyl-CoA	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P31572	-	-

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Release 2023.1 (January 2023)