5o1m

From Proteopedia

(Difference between revisions)

Revision as of 12:16, 26 August 2020

Structure of Latex Clearing Protein LCP in the closed state

Structural highlights

5o1m is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	5o1l
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).^[1] ^[2] ^[3] ^[4] ^[5]

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^[6]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Rose K, Tenberge KB, Steinbuchel A. Identification and characterization of genes from Streptomyces sp. strain K30 responsible for clear zone formation on natural rubber latex and poly(cis-1,4-isoprene) rubber degradation. Biomacromolecules. 2005 Jan-Feb;6(1):180-8. PMID:15638519 doi:http://dx.doi.org/10.1021/bm0496110
↑ Yikmis M, Arenskotter M, Rose K, Lange N, Wernsmann H, Wiefel L, Steinbuchel A. Secretion and transcriptional regulation of the latex-clearing protein, Lcp, by the rubber-degrading bacterium Streptomyces sp. strain K30. Appl Environ Microbiol. 2008 Sep;74(17):5373-82. doi: 10.1128/AEM.01001-08. Epub , 2008 Jul 7. PMID:18606806 doi:http://dx.doi.org/10.1128/AEM.01001-08
↑ Yikmis M, Steinbuchel A. Importance of the latex-clearing protein (Lcp) for poly(cis-1,4-isoprene) rubber cleavage in Streptomyces sp. K30. Microbiologyopen. 2012 Mar;1(1):13-24. doi: 10.1002/mbo3.3. PMID:22950008 doi:http://dx.doi.org/10.1002/mbo3.3
↑ Birke J, Jendrossek D. Rubber oxygenase and latex clearing protein cleave rubber to different products and use different cleavage mechanisms. Appl Environ Microbiol. 2014 Aug;80(16):5012-20. doi: 10.1128/AEM.01271-14. Epub , 2014 Jun 6. PMID:24907333 doi:http://dx.doi.org/10.1128/AEM.01271-14
↑ Birke J, Rother W, Jendrossek D. Latex Clearing Protein (Lcp) of Streptomyces sp. Strain K30 Is a b-Type Cytochrome and Differs from Rubber Oxygenase A (RoxA) in Its Biophysical Properties. Appl Environ Microbiol. 2015 Jun;81(11):3793-9. doi: 10.1128/AEM.00275-15. Epub, 2015 Mar 27. PMID:25819959 doi:http://dx.doi.org/10.1128/AEM.00275-15
↑ 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. 2017 Jul 21;7(1):6179. doi: 10.1038/s41598-017-05268-2. PMID:28733658 doi:http://dx.doi.org/10.1038/s41598-017-05268-2

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5o1m"

@@ Line 1: / Line 1: @@
 ==Structure of Latex Clearing Protein LCP in the closed state==
-<StructureSection load='5o1m' size='340' side='right' caption='[[5o1m]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
+<StructureSection load='5o1m' size='340' side='right'caption='[[5o1m]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5o1m]] is a 2 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5O1M FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5o1m]] is a 2 chain structure. 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 [http://proteopedia.org/fgij/fg.htm?mol=5O1M FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
+</td></tr><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>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5o1l|5o1l]]</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=5o1m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5o1m OCA], [http://pdbe.org/5o1m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5o1m RCSB], [http://www.ebi.ac.uk/pdbsum/5o1m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5o1m ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5o1m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5o1m OCA], [http://pdbe.org/5o1m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5o1m RCSB], [http://www.ebi.ac.uk/pdbsum/5o1m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5o1m ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 23: / Line 23: @@
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Birke, J]]
 [[Category: Brausemann, A]]

5o1m

From Proteopedia

Revision as of 12:16, 26 August 2020

Structure of Latex Clearing Protein LCP in the closed state

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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