5c9p: Difference between revisions

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<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=5c9p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c9p OCA], [http://pdbe.org/5c9p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5c9p RCSB], [http://www.ebi.ac.uk/pdbsum/5c9p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5c9p ProSAT]</span></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=5c9p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c9p OCA], [http://pdbe.org/5c9p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5c9p RCSB], [http://www.ebi.ac.uk/pdbsum/5c9p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5c9p ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Photorhabdus luminescens is known for its symbiosis with the entomopathogenic nematode Heterorhabditis bacteriophora and its pathogenicity towards insect larvae. A hypothetical protein from P. luminescens was identified, purified from the native source and characterized as an L-fucose-binding lectin, named PLL. Glycan array and biochemical characterization data revealed PLL to be specific towards L-fucose and the disaccharide glycan 3,6-O-Me2-Glcbeta1-4(2,3-O-Me2)Rhaalpha-O-(p-C6H4)-OCH2CH2NH2. PLL was discovered to be a homo-tetramer with an inter-subunit disulphide bridge. The crystal structures of native (ntPLL) and recombinant PLL (rPLL) revealed a seven-bladed beta-propeller fold creating 7 putative fucose-binding sites per monomer. The crystal structure of the rPLL/L-fucose complex confirmed at least three sites being fucose-binding. Moreover, the crystal structures indicated that some of the other sites are masked either by the tetrameric nature of the lectin or by incorporation of the C-terminus of the lectin into one of these sites. PLL exhibited a binding ability to insect haemocytes and the cuticular surface of a nematode, Heterorhabditis bacteriophora.
A Novel Fucose-Binding Lectin from Photorhabdus luminescens (PLL) with an Unusual Hepta-Bladed beta-Propeller Tetrameric Structure.,Kumar A, Sykorova P, Demo G, Dobes P, Hyrsl P, Wimmerova M J Biol Chem. 2016 Oct 7. pii: jbc.M115.693473. PMID:27758853<ref>PMID:27758853</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5c9p" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
</StructureSection>

Revision as of 14:07, 2 November 2016

Crystal structure of recombinant PLL lectin complexed with L-fucose from Photorhabdus luminescens at 1.75 A resolutionCrystal structure of recombinant PLL lectin complexed with L-fucose from Photorhabdus luminescens at 1.75 A resolution

Structural highlights

5c9p is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

Photorhabdus luminescens is known for its symbiosis with the entomopathogenic nematode Heterorhabditis bacteriophora and its pathogenicity towards insect larvae. A hypothetical protein from P. luminescens was identified, purified from the native source and characterized as an L-fucose-binding lectin, named PLL. Glycan array and biochemical characterization data revealed PLL to be specific towards L-fucose and the disaccharide glycan 3,6-O-Me2-Glcbeta1-4(2,3-O-Me2)Rhaalpha-O-(p-C6H4)-OCH2CH2NH2. PLL was discovered to be a homo-tetramer with an inter-subunit disulphide bridge. The crystal structures of native (ntPLL) and recombinant PLL (rPLL) revealed a seven-bladed beta-propeller fold creating 7 putative fucose-binding sites per monomer. The crystal structure of the rPLL/L-fucose complex confirmed at least three sites being fucose-binding. Moreover, the crystal structures indicated that some of the other sites are masked either by the tetrameric nature of the lectin or by incorporation of the C-terminus of the lectin into one of these sites. PLL exhibited a binding ability to insect haemocytes and the cuticular surface of a nematode, Heterorhabditis bacteriophora.

A Novel Fucose-Binding Lectin from Photorhabdus luminescens (PLL) with an Unusual Hepta-Bladed beta-Propeller Tetrameric Structure.,Kumar A, Sykorova P, Demo G, Dobes P, Hyrsl P, Wimmerova M J Biol Chem. 2016 Oct 7. pii: jbc.M115.693473. PMID:27758853[1]

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

References

  1. Kumar A, Sykorova P, Demo G, Dobes P, Hyrsl P, Wimmerova M. A Novel Fucose-Binding Lectin from Photorhabdus luminescens (PLL) with an Unusual Hepta-Bladed beta-Propeller Tetrameric Structure. J Biol Chem. 2016 Oct 7. pii: jbc.M115.693473. PMID:27758853 doi:http://dx.doi.org/10.1074/jbc.M115.693473

5c9p, resolution 1.75Å

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