4lk6: Difference between revisions
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==Crystal Structure of Pseudomonas aeruginosa Lectin LecA Complexed with Chlorophenol Red-b-D-galactopyranoside at 2.86 A Resolution== | |||
<StructureSection load='4lk6' size='340' side='right'caption='[[4lk6]], [[Resolution|resolution]] 2.86Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4lk6]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LK6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LK6 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.859Å</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=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=LRD:2-[(E)-(3-CHLORO-4-HYDROXYPHENYL)(3-CHLORO-4-OXOCYCLOHEXA-2,5-DIEN-1-YLIDENE)METHYL]BENZENESULFONIC+ACID'>LRD</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4lk6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lk6 OCA], [https://pdbe.org/4lk6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lk6 RCSB], [https://www.ebi.ac.uk/pdbsum/4lk6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lk6 ProSAT]</span></td></tr> | |||
</table> | |||
== 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;"> | |||
== Publication Abstract from PubMed == | |||
The galactose specific lectin LecA mediates biofilm formation in the opportunistic pathogen P. aeruginosa . The interaction between LecA and aromatic beta-galactoside biofilm inhibitors involves an intermolecular CH-pi T-shape interaction between C(epsilon1)-H of residue His50 in LecA and the aromatic ring of the galactoside aglycone. The generality of this interaction was tested in a diverse family of beta-galactosides. LecA binding to aromatic beta-galactosides (KD approximately 8 muM) was consistently stronger than to aliphatic beta-galactosides (KD approximately 36 muM). The CH-pi interaction was observed in the X-ray crystal structures of six different LecA complexes, with shorter than the van der Waals distances indicating productive binding. Related XH/cation/pi-pi interactions involving other residues were identified in complexes of aromatic glycosides with a variety of carbohydrate binding proteins such as concanavalin A. Exploiting such interactions might be generally useful in drug design against these targets. | |||
CH-pi "T-Shape" Interaction with Histidine Explains Binding of Aromatic Galactosides to Pseudomonas aeruginosa Lectin LecA.,Kadam RU, Garg D, Schwartz J, Visini R, Sattler M, Stocker A, Darbre T, Reymond JL ACS Chem Biol. 2013 Sep 20;8(9):1925-30. doi: 10.1021/cb400303w. Epub 2013 Jul, 31. PMID:23869965<ref>PMID:23869965</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4lk6" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Galactose-binding lectin|Galactose-binding lectin]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Pseudomonas aeruginosa PAO1]] | |||
[[Category: Kadam RU]] | |||
[[Category: Reymond JL]] | |||
[[Category: Stocker A]] | |||
Latest revision as of 17:35, 8 November 2023
Crystal Structure of Pseudomonas aeruginosa Lectin LecA Complexed with Chlorophenol Red-b-D-galactopyranoside at 2.86 A ResolutionCrystal Structure of Pseudomonas aeruginosa Lectin LecA Complexed with Chlorophenol Red-b-D-galactopyranoside at 2.86 A Resolution
Structural highlights
FunctionPA1L_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 mediates biofilm formation in the opportunistic pathogen P. aeruginosa . The interaction between LecA and aromatic beta-galactoside biofilm inhibitors involves an intermolecular CH-pi T-shape interaction between C(epsilon1)-H of residue His50 in LecA and the aromatic ring of the galactoside aglycone. The generality of this interaction was tested in a diverse family of beta-galactosides. LecA binding to aromatic beta-galactosides (KD approximately 8 muM) was consistently stronger than to aliphatic beta-galactosides (KD approximately 36 muM). The CH-pi interaction was observed in the X-ray crystal structures of six different LecA complexes, with shorter than the van der Waals distances indicating productive binding. Related XH/cation/pi-pi interactions involving other residues were identified in complexes of aromatic glycosides with a variety of carbohydrate binding proteins such as concanavalin A. Exploiting such interactions might be generally useful in drug design against these targets. CH-pi "T-Shape" Interaction with Histidine Explains Binding of Aromatic Galactosides to Pseudomonas aeruginosa Lectin LecA.,Kadam RU, Garg D, Schwartz J, Visini R, Sattler M, Stocker A, Darbre T, Reymond JL ACS Chem Biol. 2013 Sep 20;8(9):1925-30. doi: 10.1021/cb400303w. Epub 2013 Jul, 31. PMID:23869965[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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