1BDO

STRUCTURE OF THE BIOTINYL DOMAIN OF ACETYL-COENZYME A CARBOXYLASE DETERMINED BY MAD PHASING

Summary for 1BDO

Entry DOI	10.2210/pdb1bdo/pdb
Descriptor	ACETYL-COA CARBOXYLASE, BIOTIN (3 entities in total)
Functional Keywords	bccpsc, carboxyl transferase, fatty acid biosynthesis, hammerhead structure, selenomethionine, ligase, transferase
Biological source	Escherichia coli
Total number of polymer chains	1
Total formula weight	8944.33
Authors	Athappilly, F.K.,Hendrickson, W.A. (deposition date: 1995-11-21, release date: 1996-08-01, Last modification date: 2024-10-23)
Primary citation	Athappilly, F.K.,Hendrickson, W.A. Structure of the biotinyl domain of acetyl-coenzyme A carboxylase determined by MAD phasing. Structure, 3:1407-1419, 1995 Cited by PubMed Abstract: Acetyl-coenzyme A carboxylase catalyzes the first committed step of fatty acid biosynthesis. Universally, this reaction involves three functional components all related to a carboxybiotinyl intermediate. A biotinyl domain shuttles its covalently attached biotin prosthetic group between the active sites of a biotin carboxylase and a carboxyl transferase. In Escherichia coli, the three components reside in separate subunits: a biotinyl domain is the functional portion of one of these, biotin carboxy carrier protein (BCCP). PubMed: 8747466 DOI: 10.1016/S0969-2126(01)00277-5 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.8 Å)

Structure validation