5o1l
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of Latex Clearing Protein LCP in the open state with bound imidazole== | |
| + | <StructureSection load='5o1l' size='340' side='right' caption='[[5o1l]], [[Resolution|resolution]] 1.48Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5o1l]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5O1L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5O1L FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BU3:(R,R)-2,3-BUTANEDIOL'>BU3</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5o1m|5o1m]]</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5o1l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5o1l OCA], [http://pdbe.org/5o1l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5o1l RCSB], [http://www.ebi.ac.uk/pdbsum/5o1l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5o1l ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/LCP_STRK3 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).<ref>PMID:15638519</ref> <ref>PMID:18606806</ref> <ref>PMID:22950008</ref> <ref>PMID:24907333</ref> <ref>PMID:25819959</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:28733658</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 5o1l" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Birke, J]] | [[Category: Birke, J]] | ||
| - | [[Category: | + | [[Category: Brausemann, A]] |
[[Category: Einsle, O]] | [[Category: Einsle, O]] | ||
[[Category: Ilcu, L]] | [[Category: Ilcu, L]] | ||
| + | [[Category: Jendrossek, D]] | ||
| + | [[Category: Roether, W]] | ||
| + | [[Category: Biopolymer]] | ||
| + | [[Category: Heme]] | ||
| + | [[Category: Oxidoreductase]] | ||
| + | [[Category: Oxygenase]] | ||
| + | [[Category: Rubber]] | ||
Revision as of 04:15, 4 August 2017
Structure of Latex Clearing Protein LCP in the open state with bound imidazole
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Categories: Birke, J | Brausemann, A | Einsle, O | Ilcu, L | Jendrossek, D | Roether, W | Biopolymer | Heme | Oxidoreductase | Oxygenase | Rubber
