5o1m

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(New page: '''Unreleased structure''' The entry 5o1m is ON HOLD Authors: Ilcu, L., Roether, W., Birke, J., Brausemann, A., Einsle, O., Jendrossek, D. Description: Structure of Latex Clearing Prot...)
Current revision (19:03, 29 November 2023) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 5o1m is ON HOLD
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==Structure of Latex Clearing Protein LCP in the closed state==
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<StructureSection load='5o1m' size='340' side='right'caption='[[5o1m]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5o1m]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_sp._K30 Streptomyces sp. K30]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5O1M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5O1M FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5o1m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5o1m OCA], [https://pdbe.org/5o1m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5o1m RCSB], [https://www.ebi.ac.uk/pdbsum/5o1m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5o1m ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors: Ilcu, L., Roether, W., Birke, J., Brausemann, A., Einsle, O., Jendrossek, D.
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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>
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Description: Structure of Latex Clearing Protein LCP in the closed state
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Roether, W]]
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<div class="pdbe-citations 5o1m" style="background-color:#fffaf0;"></div>
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[[Category: Brausemann, A]]
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== References ==
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[[Category: Birke, J]]
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<references/>
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[[Category: Jendrossek, D]]
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__TOC__
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[[Category: Einsle, O]]
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</StructureSection>
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[[Category: Ilcu, L]]
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[[Category: Large Structures]]
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[[Category: Streptomyces sp. K30]]
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[[Category: Birke J]]
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[[Category: Brausemann A]]
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[[Category: Einsle O]]
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[[Category: Ilcu L]]
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[[Category: Jendrossek D]]
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[[Category: Roether W]]

Current revision

Structure of Latex Clearing Protein LCP in the closed state

PDB ID 5o1m

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