5o1l

Structure of Latex Clearing Protein LCP in the open state with bound imidazole

spinqualitylabelsall models 5o1l, resolution 1.48Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5o1l is a 2 chain structure with sequence from Streptomyces sp. K30. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.48Å Ligands: BU3, EDO, HEM, IMD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function LCP_STRK3 Involved in the initial step of rubber degradation (PubMed:22950008, PubMed:15638519, PubMed:18606806). Catalyzes the oxidative C-C cleavage of poly(cis-1,4-isoprene) in synthetic as well as in natural rubber by the addition of oxygen (O2) to the double bonds, leading to a mixture of oligonucleotide-isoprenoids with terminal keto and aldehyde groups (endo-type cleavage) (PubMed:25819959, PubMed:24907333). The cleavage products are of different lengths, ranging from C20 (four isoprene units) to higher oligo-isoprenoids (PubMed:24907333). Is not able to cleave low-molecular-weight substrate analogs with isoprenoid structure such as squalene (1,4-trans-isoprenoid), carotenoids, or alpha-tocopherol (PubMed:24907333). Publication Abstract from PubMed 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 (LcpK30) is a b-type cytochrome and acts as an endo-type dioxygenase producing C20 and higher oligo-isoprenoids that differ in the number of isoprene units but have the same terminal functions, CHO-CH2- and -CH2-COCH3. 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 LcpK30 is ligated to the polypeptide by a proximal histidine (His198) and by a lysine residue (Lys167) as the distal axial ligand. The comparison of LcpK30 structures in a closed and in an open state as well as spectroscopic and biochemical analysis of wild type and LcpK30 muteins provided insights into the action of the enzyme during catalysis. Structural and Functional Analysis of Latex Clearing Protein (Lcp) Provides Insight into the Enzymatic Cleavage of Rubber.,Ilcu L, Rother W, Birke J, Brausemann A, Einsle O, Jendrossek D Sci Rep. 2017 Jul 21;7(1):6179. doi: 10.1038/s41598-017-05268-2. PMID:28733658 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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