scholarly journals A bivalent glycopeptide to target two putative carbohydrate binding sites on FimH

2010 ◽  
Vol 6 ◽  
pp. 801-809 ◽  
Author(s):  
Thisbe K Lindhorst ◽  
Kathrin Bruegge ◽  
Andreas Fuchs ◽  
Oliver Sperling
Keyword(s):  
Binding Site ◽  
Binding Sites ◽  
Carbohydrate Binding ◽  
Carbohydrate Recognition Domain ◽  
Carbohydrate Recognition ◽  
Binding Studies ◽  
Bivalent Ligand ◽  
X Ray ◽  
Carbohydrate Binding Site

FimH is a mannose-specific bacterial lectin found on type 1 fimbriae with a monovalent carbohydrate recognition domain (CRD) that is known from X-ray studies. However, binding studies with multivalent ligands have suggested an additional carbohydrate-binding site on this protein. In order to prove this hypothesis, a bivalent glycopeptide ligand with the capacity to bridge two putative carbohydrate binding sites on FimH was designed and synthesized. Anti-adhesion assays with the new bivalent ligand and type 1-fimbriated bacteria have revealed, that verification of the number of carbohydrate binding sites on FimH with a tailor-made bivalent glycopeptide requires further investigation to be conclusive.

scholarly journals Are D-manno-configured Amadori products ligands of the bacterial lectin FimH?

2015 ◽  
Vol 11 ◽  
pp. 1096-1104 ◽  
Author(s):  
Tobias-Elias Gloe ◽  
Insa Stamer ◽  
Cornelia Hojnik ◽  
Tanja M Wrodnigg ◽  
Thisbe K Lindhorst
Keyword(s):  
Molecular Docking ◽  
Binding Site ◽  
Bacterial Adhesion ◽  
Carbohydrate Binding ◽  
Amadori Products ◽  
E Coli ◽  
Type D ◽  
Amadori Rearrangement ◽  
Carbohydrate Binding Site

The Amadori rearrangement was employed for the synthesis ofC-glycosyl-type D-mannoside analogues, namely 1-propargylamino- and 1-phenylamino-1-deoxy-α-D-manno-heptopyranose. They were investigated as ligands of type 1-fimbriatedE. colibacteria by means of molecular docking and bacterial adhesion studies. It turns out that Amadori rearrangement products have a limited activity as inhibitors of bacterial adhesion because the β-C-glycosidically linked aglycone considerably hampers complexation within the carbohydrate binding site of the type 1-fimbrial lectin FimH.

scholarly journals Structural Basis for Recognition of High Mannose Type Glycoproteins by Mammalian Transport Lectin VIP36

2007 ◽  
Vol 282 (38) ◽  
pp. 28246-28255 ◽  
Author(s):  
Tadashi Satoh ◽  
Nathan P. Cowieson ◽  
Wataru Hakamata ◽  
Hiroko Ideo ◽  
Keiko Fukushima ◽  
...  
Keyword(s):  
Secretory Pathway ◽  
Structural Basis ◽  
Carbohydrate Binding ◽  
Carbohydrate Recognition Domain ◽  
Complex Structures ◽  
Carbohydrate Recognition ◽  
Specific Manner ◽  
Stalk Domain ◽  
High Mannose ◽  
Carbohydrate Binding Site

VIP36 functions as a transport lectin for trafficking certain high mannose type glycoproteins in the secretory pathway. Here we report the crystal structure of VIP36 exoplasmic/luminal domain comprising a carbohydrate recognition domain and a stalk domain. The structures of VIP36 in complex with Ca2+ and mannosyl ligands are also described. The carbohydrate recognition domain is composed of a 17-stranded antiparallel β-sandwich and binds one Ca2+ adjoining the carbohydrate-binding site. The structure reveals that a coordinated Ca2+ ion orients the side chains of Asp131, Asn166, and His190 for carbohydrate binding. This result explains the Ca2+-dependent carbohydrate binding of this protein. The Man-α-1,2-Man-α-1,2-Man, which corresponds to the D1 arm of high mannose type glycan, is recognized by eight residues through extensive hydrogen bonds. The complex structures reveal the structural basis for high mannose type glycoprotein recognition by VIP36 in a Ca2+-dependent and D1 arm-specific manner.

scholarly journals Structure of Dioclea virgata lectin: Relations between carbohydrate binding site and nitric oxide production

Biochimie ◽  
2012 ◽  
Vol 94 (3) ◽  
pp. 900-906 ◽  
Author(s):  
Raphael Batista da Nóbrega ◽  
Bruno A.M. Rocha ◽  
Carlos Alberto A. Gadelha ◽  
Tatiane Santi-Gadelha ◽  
Alana F. Pires ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Binding Site ◽  
Carbohydrate Binding ◽  
Nitric Oxide Production ◽  
Oxide Production ◽  
Carbohydrate Binding Site

Structural basis of carbohydrate binding in domain C of a type I pullulanase from Paenibacillus barengoltzii

2020 ◽  
Vol 76 (5) ◽  
pp. 447-457
Author(s):  
Ping Huang ◽  
Shiwang Wu ◽  
Shaoqing Yang ◽  
Qiaojuan Yan ◽  
Zhengqiang Jiang
Keyword(s):  
Binding Site ◽  
Binding Sites ◽  
Structural Basis ◽  
Carbohydrate Binding ◽  
Type I ◽  
Debranching Enzyme ◽  
Crystal Forms ◽  
Aromatic Residues ◽  
Starch Debranching Enzyme ◽  
Paenibacillus Barengoltzii

Pullulanase (EC 3.2.1.41) is a well known starch-debranching enzyme that catalyzes the cleavage of α-1,6-glycosidic linkages in α-glucans such as starch and pullulan. Crystal structures of a type I pullulanase from Paenibacillus barengoltzii (PbPulA) and of PbPulA in complex with maltopentaose (G5), maltohexaose (G6)/α-cyclodextrin (α-CD) and β-cyclodextrin (β-CD) were determined in order to better understand substrate binding to this enzyme. PbPulA belongs to glycoside hydrolase (GH) family 13 subfamily 14 and is composed of three domains (CBM48, A and C). Three carbohydrate-binding sites identified in PbPulA were located in CBM48, near the active site and in domain C, respectively. The binding site in CBM48 was specific for β-CD, while that in domain C has not been reported for other pullulanases. The domain C binding site had higher affinity for α-CD than for G6; a small motif (FGGEH) seemed to be one of the major determinants for carbohydrate binding in this domain. Structure-based mutations of several surface-exposed aromatic residues in CBM48 and domain C had a debilitating effect on the activity of the enzyme. These results suggest that both CBM48 and domain C play a role in binding substrates. The crystal forms described contribute to the understanding of pullulanase domain–carbohydrate interactions.

Characterisation of Metal Binding Sites for 8-Azaguanine and 8-Azahypoxanthine Derivatives Synthesis and X-Ray Structural Analysis of Methylmercury(II) and Zinc(II) Complexes

1986 ◽  
Vol 41 (9) ◽  
pp. 1117-1122 ◽  
Author(s):  
W. S. Sheldrick ◽  
P. Bell
Keyword(s):  
Structural Analysis ◽  
Binding Site ◽  
Metal Binding ◽  
Binding Sites ◽  
Antineoplastic Agent ◽  
X Ray ◽  
Metal Binding Sites ◽  
Ph Values ◽  
Ph Range

Abstract The complexes [(CH3Hg)AGuaH ] (1) and [(CH3Hg)2AGua] • H2O (2) have been isolated from aqueous 1:1 and 2:1 solutions of CH3HgOH and 8 -azaguanine (AGuaH2) at respective pH values of 5 and 9. Only one CH3Hg+ complex of 8 -azahypoxanthine (AHxH2), namely [(CH3Hg)2AHx] (3), could be isolated under analogous conditions. X-ray structural analyses established N1 and N9 as metal binding sites in 3 and N9 as the coordination position in [Zn(H2O)4(AHxH)2] (4). With 8-aza-9-benzylhypoxanthine (9-BzAHxH) only one CH3Hg+ complex [(CH3Hg)9-BzAHx] (5) could be isolated in the pH range 2-10. N1 was established by X-ray structural analysis as the binding site. The relevance o f these findings to an understanding of ligand behaviour of the antineoplastic agent 8 -azaguanine is discussed.

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