4al9: Difference between revisions
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<StructureSection load='4al9' size='340' side='right'caption='[[4al9]], [[Resolution|resolution]] 1.75Å' scene=''> | <StructureSection load='4al9' size='340' side='right'caption='[[4al9]], [[Resolution|resolution]] 1.75Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4al9]] is a 8 chain structure | <table><tr><td colspan='2'>[[4al9]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AL9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AL9 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GLA:ALPHA+D-GALACTOSE'>GLA</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GLA:ALPHA+D-GALACTOSE'>GLA</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1l7l|1l7l]], [[1oko|1oko]], [[1uoj|1uoj]], [[2vxj|2vxj]], [[2wyf|2wyf]], [[3zyb|3zyb]], [[3zyf|3zyf]], [[3zyh|3zyh]], [[4a6s|4a6s]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1l7l|1l7l]], [[1oko|1oko]], [[1uoj|1uoj]], [[2vxj|2vxj]], [[2wyf|2wyf]], [[3zyb|3zyb]], [[3zyf|3zyf]], [[3zyh|3zyh]], [[4a6s|4a6s]]</div></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4al9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4al9 OCA], [https://pdbe.org/4al9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4al9 RCSB], [https://www.ebi.ac.uk/pdbsum/4al9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4al9 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/PA1L_PSEAE PA1L_PSEAE]] D-galactose specific lectin. Binds in decreasing order of affinity: melibiose, methyl-alpha-D-galactoside, D-galactose, methyl-beta-D-galactoside, N-acetyl-D-galactosamine. Similar to plant lectins in its selective (carbohydrate-specific) hemagglutinating activity. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Blanchard, B]] | [[Category: Blanchard, B]] | ||
[[Category: Imberty, A]] | [[Category: Imberty, A]] | ||
Revision as of 08:37, 25 August 2022
Crystal structure of the lectin PA-IL from Pseudomonas aeruginoas in complex with melibioseCrystal structure of the lectin PA-IL from Pseudomonas aeruginoas in complex with melibiose
Structural highlights
Function[PA1L_PSEAE] D-galactose specific lectin. Binds in decreasing order of affinity: melibiose, methyl-alpha-D-galactoside, D-galactose, methyl-beta-D-galactoside, N-acetyl-D-galactosamine. Similar to plant lectins in its selective (carbohydrate-specific) hemagglutinating activity. Publication Abstract from PubMedThe galactose-specific lectin LecA from Pseudomonas aeruginosa is a target for the development of new anti-infectious compounds. Sugar based molecules with anti-adhesive properties present great potential in the fight against bacterial infection and biofilm formation. LecA is specific for oligosaccharides with terminal alpha-galactoside residues and displays strong affinity for melibiose (alphaGal1-6Glc) with a Kd of 38.8 microM. The crystal structure of LecA/melibiose complex shows classical calcium-bridged binding of alphaGal in the primary binding site but also revealed a secondary sugar binding site with glucose bound. This sugar binding site is in close proximity to the galactose binding one, is independent of calcium and mainly involves interactions with a symmetry-related protein. This discovery would help to the design of new potent inhibitors targeting both binding sites. Secondary sugar binding site identified for LecA lectin from Pseudomonas aeruginosa.,Blanchard B, Imberty A, Varrot A Proteins. 2013 Oct 1. doi: 10.1002/prot.24430. PMID:24123124[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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