5O1M

Structure of Latex Clearing Protein LCP in the closed state

Summary for 5O1M

• Entry DOI: 10.2210/pdb5o1m/pdb
• Related: 5o1l
• Descriptor: Rubber oxygenase, PROTOPORPHYRIN IX CONTAINING FE, 1,2-ETHANEDIOL, ... (4 entities in total)
• Functional Keywords: heme, oxygenase, rubber, biopolymers, oxidoreductase
• Biological source: Streptomyces sp. (strain K30)
• Cellular location: Secreted : Q3L8N0
• Total number of polymer chains: 2
• Total formula weight: 82049.67

Authors

Ilcu, L.,Roether, W.,Birke, J.,Brausemann, A.,Einsle, O.,Jendrossek, D. (deposition date: 2017-05-18, release date: 2017-08-02, Last modification date: 2024-05-08)

Primary citation

Ilcu, L.,Rother, W.,Birke, J.,Brausemann, A.,Einsle, O.,Jendrossek, D.
Structural and Functional Analysis of Latex Clearing Protein (Lcp) Provides Insight into the Enzymatic Cleavage of Rubber.
Sci Rep, 7:6179-6179, 2017

PubMed Abstract: 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.

PubMed: 28733658
DOI: 10.1038/s41598-017-05268-2

Experimental method

X-RAY DIFFRACTION (2.2 Å)