期刊
SCIENTIFIC REPORTS
卷 7, 期 -, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/s41598-017-05268-2
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资金
- Deutsche Forschungsgemeinschaft [Ei-520/5, Je-152/18]
- Deutscher Akademischer Austauschdienst
Latex clearing proteins (Lcps) are rubber oxygenases that catalyse the extracellular cleavage of poly (cis-1,4-isoprene) by Gram-positive rubber degrading bacteria. Lcp of Streptomyces sp. K30 (Lcp(K30)) is a b-type cytochrome and acts as an endo-type dioxygenase producing C-20 and higher oligo-isoprenoids that differ in the number of isoprene units but have the same terminal functions, CHO-CH2-and-CH2COCH3. Our analysis of the LcpK30 structure revealed a 3/3 globin fold with additional domains at the N-and C-termini and similarities to globin-coupled sensor proteins. The haem group of Lcp(K30) is ligated to the polypeptide by a proximal histidine (His198) and by a lysine residue (Lys167) as the distal axial ligand. The comparison of Lcp(K30) structures in a closed and in an open state as well as spectroscopic and biochemical analysis of wild type and Lcp(K30) muteins provided insights into the action of the enzyme during catalysis.
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