Structural characterization of the entire 1.3S subunit of transcarboxylase from Propionibacterium shermanii.
Structural characterization of the entire 1.3S subunit of transcarboxylase from Propionibacterium shermanii.
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谢尔曼丙酸杆菌转羧酶整个 1.3S 亚基的结构表征。
DOI：
10.1002/pro.5560071013
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发表时间：
1998
期刊：
影响因子：
--
通讯作者：
Sönnichsen,FD
中科院分区：
文献类型：
--
作者：
Reddy,DV;Rothemund,S;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 in two partial reactions. Within the multisubunit enzyme complex, the 1.3S subunit functions as the carboxyl group carrier. The 1.3S is a 123‐amino acid polypeptide (12.6 kDa), to which biotin is covalently attached at Lys 89. We have expressed 1.3S inEscherichia coliwith uniform15N labeling. The backbone structure and dynamics of the protein have been characterized in aqueous solution by three‐dimensional heteronuclear nuclear magnetic resonance (NMR) spectroscopy. The secondary structure elements in the protein were identified based on NOE information, secondary chemical shifts, homonuclear3Jhnhα coupling constants, and amide proton exchange data. The protein contains a predominantly disordered N‐terminal half, while the C‐terminal half is folded into a compact domain comprising eight β‐strands connected by short loops and turns. The topology of the C‐terminal domain is consistent with the fold found in both carboxyl carrier and lipoyl domains, to which this domain has approximately 26‐30% sequence similarity.
