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) is a b-type cytochrome and acts as an endo-type dioxygenase producing C and higher oligo-isoprenoids that differ in the number of isoprene units but have the same terminal functions, CHO-CH- and -CH-COCH. Our analysis of the Lcp 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 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 structures in a closed and in an open state as well as spectroscopic and biochemical analysis of wild type and Lcp muteins provided insights into the action of the enzyme during catalysis.
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| http://dx.doi.org/10.1038/s41598-017-05268-2 | DOI Listing |
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