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1iqb

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Revision as of 09:19, 29 September 2021

Crystal Structure of Urtica dioica Agglutinin Isolectin I

Structural highlights

1iqb is a 2 chain structure with sequence from Urtica dioica. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[AGI_URTDI] Functions both as a chitinase and as a N-acetyl-D-glucosamine binding lectin. Inhibits the growth of several phytopathogenic chitin-containing fungi. Possesses also insecticidal activity and superantigenic properties.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Ultica dioica agglutinin, a plant lectin from the stinging nettle, consists of a total of seven individual isolectins. One of these structures, isolectin I, was determined at 1.9 A resolution by the X-ray method. The crystals belong to the space group P2(1) and the asymmetric unit contains two molecules related by local twofold symmetry. The molecule consists of two hevein-like chitin-binding domains lacking distinct secondary structure, but four disulfide bonds in each domain maintain the tertiary structure. The backbone structure of the two independent molecules is essentially identical and this is similarly true of the sugar-binding sites. In the crystal, the C-terminal domains bind Zn(2+) ions at the sugar-binding site. Owing to their location near a pseudo-twofold axis, the two zinc ions link the two independent molecules in a tail-to-tail arrangement: thus, His47 of molecule 1 and His67 of molecule 2 coordinate the first zinc ion, while the second zinc ion links Asp75 of molecule 1 and His47 of molecule 2.

Structure of Urtica dioica agglutinin isolectin I: dimer formation mediated by two zinc ions bound at the sugar-binding site.,Harata K, Schubert WD, Muraki M Acta Crystallogr D Biol Crystallogr. 2001 Nov;57(Pt 11):1513-7. Epub 2001, Oct 25. PMID:11679714^[2]

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

References

↑ Saul FA, Rovira P, Boulot G, Damme EJ, Peumans WJ, Truffa-Bachi P, Bentley GA. Crystal structure of Urtica dioica agglutinin, a superantigen presented by MHC molecules of class I and class II. Structure. 2000 Jun 15;8(6):593-603. PMID:10873861
↑ Harata K, Schubert WD, Muraki M. Structure of Urtica dioica agglutinin isolectin I: dimer formation mediated by two zinc ions bound at the sugar-binding site. Acta Crystallogr D Biol Crystallogr. 2001 Nov;57(Pt 11):1513-7. Epub 2001, Oct 25. PMID:11679714

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1iqb"

@@ Line 3: / Line 3: @@
 <StructureSection load='1iqb' size='340' side='right'caption='[[1iqb]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1iqb]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Urtica_dioica Urtica dioica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IQB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IQB FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1iqb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Urtica_dioica Urtica dioica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IQB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IQB FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></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=1iqb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iqb OCA], [http://pdbe.org/1iqb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1iqb RCSB], [http://www.ebi.ac.uk/pdbsum/1iqb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1iqb ProSAT]</span></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=1iqb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iqb OCA], [https://pdbe.org/1iqb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iqb RCSB], [https://www.ebi.ac.uk/pdbsum/1iqb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iqb ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/AGI_URTDI AGI_URTDI]] Functions both as a chitinase and as a N-acetyl-D-glucosamine binding lectin. Inhibits the growth of several phytopathogenic chitin-containing fungi. Possesses also insecticidal activity and superantigenic properties.<ref>PMID:10873861</ref>
+[[https://www.uniprot.org/uniprot/AGI_URTDI AGI_URTDI]] Functions both as a chitinase and as a N-acetyl-D-glucosamine binding lectin. Inhibits the growth of several phytopathogenic chitin-containing fungi. Possesses also insecticidal activity and superantigenic properties.<ref>PMID:10873861</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1iqb

From Proteopedia

Revision as of 09:19, 29 September 2021

Crystal Structure of Urtica dioica Agglutinin Isolectin I

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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