4lk7

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(Difference between revisions)

Revision as of 11:06, 14 December 2022

Crystal Structure of Pseudomonas aeruginosa Lectin LecA Complexed with Resorufin-b-D-galactopyranoside at 1.76 A Resolution

Structural highlights

4lk7 is a 4 chain structure with sequence from Pseudomonas aeruginosa PAO1. 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

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 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^[1]

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

References

↑ Kadam RU, Garg D, Schwartz J, Visini R, Sattler M, Stocker A, Darbre T, Reymond JL. CH-pi "T-Shape" Interaction with Histidine Explains Binding of Aromatic Galactosides to Pseudomonas aeruginosa Lectin LecA. ACS Chem Biol. 2013 Sep 20;8(9):1925-30. doi: 10.1021/cb400303w. Epub 2013 Jul, 31. PMID:23869965 doi:http://dx.doi.org/10.1021/cb400303w

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4lk7"

Categories: Large Structures | Pseudomonas aeruginosa PAO1 | Kadam RU | Reymond JL | Stocker A

@@ Line 1: / Line 1: @@
 ==Crystal Structure of Pseudomonas aeruginosa Lectin LecA Complexed with Resorufin-b-D-galactopyranoside at 1.76 A Resolution==
-<StructureSection load='4lk7' size='340' side='right' caption='[[4lk7]], [[Resolution|resolution]] 1.76&Aring;' scene=''>
+<StructureSection load='4lk7' size='340' side='right'caption='[[4lk7]], [[Resolution|resolution]] 1.76&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4lk7]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseae Pseae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LK7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LK7 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4lk7]] is a 4 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=4LK7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LK7 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=04G:7-HYDROXY-3H-PHENOXAZIN-3-ONE'>04G</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=04G:7-HYDROXY-3H-PHENOXAZIN-3-ONE'>04G</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ljh|4ljh]], [[4lk6|4lk6]]</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=4lk7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lk7 OCA], [https://pdbe.org/4lk7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lk7 RCSB], [https://www.ebi.ac.uk/pdbsum/4lk7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lk7 ProSAT]</span></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lecA, pa1L, PA2570 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=208964 PSEAE])</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=4lk7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lk7 OCA], [http://pdbe.org/4lk7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4lk7 RCSB], [http://www.ebi.ac.uk/pdbsum/4lk7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4lk7 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://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.
+[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 ==
@@ Line 27: / Line 25: @@
 __TOC__
 </StructureSection>
-[[Category: Pseae]]
+[[Category: Large Structures]]
-[[Category: Kadam, R U]]
+[[Category: Pseudomonas aeruginosa PAO1]]
-[[Category: Reymond, J L]]
+[[Category: Kadam RU]]
-[[Category: Stocker, A]]
+[[Category: Reymond JL]]
-[[Category: Galactose]]
+[[Category: Stocker A]]
-[[Category: Lectin fold]]
-[[Category: Sugar binding protein]]

4lk7

From Proteopedia

Revision as of 11:06, 14 December 2022

Crystal Structure of Pseudomonas aeruginosa Lectin LecA Complexed with Resorufin-b-D-galactopyranoside at 1.76 A Resolution

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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