1dd2
From Proteopedia
|
BIOTIN CARBOXYL CARRIER DOMAIN OF TRANSCARBOXYLASE (TC 1.3S)
Overview
Transcarboxylase (TC) from Propionibacterium shermanii, a biotin-dependent, enzyme, catalyzes the transfer of a carboxyl group from methylmalonyl-CoA, to pyruvate to form propionyl-CoA and oxalacetate. Within the, multi-subunit enzyme complex, the 1.3S subunit functions as the carboxyl, group carrier and also binds the other two subunits to assist in the, overall assembly of the enzyme. The 1.3S subunit is a 123 amino acid, polypeptide (12.6 kDa) to which biotin is covalently attached at Lys 89., The three-dimensional solution structure of the full-length holo-1.3S, subunit of TC has been solved by multidimensional heteronuclear NMR, spectroscopy. The C-terminal half of the protein (51-123) is folded into a, compact all-beta-domain comprising of two four-stranded antiparallel, beta-sheets connected by short loops and turns. The fold exhibits a high, 2-fold internal symmetry and is similar to that of the biotin carboxyl, carrier protein (BCCP) of acetyl-CoA carboxylase, but lacks an extension, that has been termed "protruding thumb" in BCCP. The first 50 residues, which have been shown to be involved in intersubunit interactions in the, intact enzyme, appear to be disordered in the isolated 1.3S subunit. The, molecular surface of the folded domain has two distinct surfaces: one side, is highly charged, while the other comprises mainly hydrophobic, highly, conserved residues.
About this Structure
1DD2 is a Single protein structure of sequence from Propionibacterium freudenreichii subsp. shermanii. Active as Methylmalonyl-CoA carboxytransferase, with EC number 2.1.3.1 Full crystallographic information is available from OCA.
Reference
High resolution solution structure of the 1.3S subunit of transcarboxylase from Propionibacterium shermanii., Reddy DV, Shenoy BC, Carey PR, Sonnichsen FD, Biochemistry. 2000 Mar 14;39(10):2509-16. PMID:10704200
Page seeded by OCA on Tue Nov 20 13:10:59 2007
