1DD2

BIOTIN CARBOXYL CARRIER DOMAIN OF TRANSCARBOXYLASE (TC 1.3S)

1DD2 の概要

• エントリーDOI: 10.2210/pdb1dd2/pdb
• 関連するPDBエントリー: 1DCZ
• NMR情報: BMRB: 4666
• 分子名称: TRANSCARBOXYLASE 1.3S SUBUNIT (1 entity in total)
• 機能のキーワード: antiparallel beta sheet, hammerhead, biocytin, transferase
• 由来する生物種: Propionibacterium freudenreichii subsp. shermanii
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 7822.06

構造登録者

Reddy, D.V.,Shenoy, B.C.,Carey, P.R.,Sonnichsen, F.D. (登録日: 1999-11-06, 公開日: 2000-03-24, 最終更新日: 2024-05-22)

主引用文献

Reddy, D.V.,Shenoy, B.C.,Carey, P.R.,Sonnichsen, F.D.
High resolution solution structure of the 1.3S subunit of transcarboxylase from Propionibacterium shermanii.
Biochemistry, 39:2509-2516, 2000

PubMed 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.

PubMed: 10704200
DOI: 10.1021/bi9925367

実験手法

SOLUTION NMR