PDBsum entry 1dd2

Transferase

PDB id: 1dd2

Contents

Protein chain

77 a.a. *

* Residue conservation analysis

References listed in PDB file

Key reference

• Title: High resolution solution structure of the 1.3s subunit of transcarboxylase from propionibacterium shermanii.
• Authors: D.V.Reddy, B.C.Shenoy, P.R.Carey, F.D.Sönnichsen.
• Ref.: Biochemistry, 2000, 39, 2509-2516. [DOI no: 10.1021/bi9925367]
• PubMed id: 10704200

Abstract

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.

Secondary reference #1

• Title: Structural characterization of the entire 1.3s subunit of transcarboxylase from propionibacterium shermanii.
• Authors: D.V.Reddy, S.Rothemund, B.C.Shenoy, P.R.Carey, F.D.Sönnichsen.
• Ref.: Protein Sci, 1998, 7, 2156-2163. [DOI no: 10.1002/pro.5560071013]
• PubMed id: 9792103

Secondary reference #2

• Title: Absence of observable biotin-Protein interactions in the 1.3s subunit of transcarboxylase: an nmr study.
• Authors: D.V.Reddy, B.C.Shenoy, P.R.Carey, F.D.Sönnichsen.
• Ref.: Biochemistry, 1997, 36, 14676-14682. [DOI no: 10.1021/bi971674y]
• PubMed id: 9398186