Mobile sequences in the pyruvate dehydrogenase complex, the E2 component, the catalytic domain and the 2‐oxoglutarate dehydrogenase complex of Azotobacter vinelandii, as detected by 600 MHz 1H‐NMR spectroscopy

FEBS Letters

Westphal, Adrie H.¹  Vervoort, Jacques¹  de Kok, Arie¹  Hanemaaijer, Roeland¹  Veeger, Cees¹ 

[1] Department of Biochemistry, Agricultural University, Dreijenlaan 3, 6703 HA Wageningen, The Netherlands

关键词: Dihydrolipoyl transacetylase;    Pyruvate dehydrogenase complex;    1H-NMR spectroscopy;    Mobility;    (Azotobacter vinelandii);   

DOI  :  10.1016/0014-5793(88)80369-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

600 MHz ¹H-NMR spectroscopy demonstrates that the pyruvate dehydrogenase complex of Azotobacter vinelandii contains regions of the polypeptide chain with intramolecular mobility. This mobility is located in the E₂ component and can probably be ascribed to alanine-proline-rich regions that link the lipoyl subdomains to each other as well as to the E₁ and E₃ binding domain. In the catalytic domain of E₂, which is thought to form a compact, rigid core, also conformational flexibility is observed. It is conceivable that the N-terminal region of the catalytic domain, which contains many alanine residues, is responsible for the observed mobility. In the low-field region of the ¹H-NMR spectrum of E₂ specific resonances are found, which can be ascribed to mobile phenylalanine, histidine and/or tyrosine residues which are located in the E₁ and E₃ binding domain that links the lipoyl domain to the catalytic domain. In the ¹H-NMR spectrum of the intact complex, these resonances cannot be observed, indicating a decreased mobility of the E₁ and E₃ binding domain.

【 授权许可】

Unknown