High resolution solution structure of the 1.3S subunit of transcarboxylase from Propionibacterium shermanii.
High resolution solution structure of the 1.3S subunit of transcarboxylase from Propionibacterium shermanii.
复制标题
谢尔曼丙酸杆菌转羧酶 1.3S 亚基的高分辨率溶液结构。
DOI：
10.1021/bi9925367
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发表时间：
2000
期刊：
影响因子：
2.9
通讯作者：
Sönnichsen,FD
中科院分区：
文献类型：
--
作者：
Reddy,DV;Shenoy,BC;Carey,PR;Sönnichsen,FD
Transcarboxylase (TC) fromPropionibacterium 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-β-domain comprising of two four-stranded antiparallel β-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.
