4fbv: Difference between revisions
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==Crystal structure of the Myxococcus Xanthus hemagglutinin in complex with a3,a6-mannopentaose== | ==Crystal structure of the Myxococcus Xanthus hemagglutinin in complex with a3,a6-mannopentaose== | ||
<StructureSection load='4fbv' size='340' side='right' caption='[[4fbv]], [[Resolution|resolution]] 1.76Å' scene=''> | <StructureSection load='4fbv' size='340' side='right'caption='[[4fbv]], [[Resolution|resolution]] 1.76Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4fbv]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4fbv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Myxococcus_xanthus Myxococcus xanthus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FBV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FBV FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</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=4fbv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fbv OCA], [https://pdbe.org/4fbv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fbv RCSB], [https://www.ebi.ac.uk/pdbsum/4fbv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fbv ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/MBHA_MYXXA MBHA_MYXXA] This lectin might have a role in the differentiation of cells. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
*[[Hemagglutinin|Hemagglutinin]] | *[[Agglutinin 3D structures|Agglutinin 3D structures]] | ||
*[[Hemagglutinin 3D structures|Hemagglutinin 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Myxococcus xanthus]] | ||
[[Category: | [[Category: Gronenborn AM]] | ||
[[Category: | [[Category: Koharudin LMI]] | ||
Revision as of 07:47, 7 October 2022
Crystal structure of the Myxococcus Xanthus hemagglutinin in complex with a3,a6-mannopentaoseCrystal structure of the Myxococcus Xanthus hemagglutinin in complex with a3,a6-mannopentaose
Structural highlights
FunctionMBHA_MYXXA This lectin might have a role in the differentiation of cells. Publication Abstract from PubMedOscillatoria agardhii agglutinin homolog (OAAH) proteins belong to a recently discovered lectin family. All members contain a sequence repeat of approximately 66 amino acids, with the number of repeats varying among different family members. Apart from data for the founding member OAA, neither three-dimensional structures, information about carbohydrate binding specificities, nor antiviral activity data have been available up to now for any other members of the OAAH family. To elucidate the structural basis for the antiviral mechanism of OAAHs, we determined the crystal structures of Pseudomonas fluorescens and Myxococcus xanthus lectins. Both proteins exhibit the same fold, resembling the founding family member, OAA, with minor differences in loop conformations. Carbohydrate binding studies by NMR and x-ray structures of glycan-lectin complexes reveal that the number of sugar binding sites corresponds to the number of sequence repeats in each protein. As for OAA, tight and specific binding to alpha3,alpha6-mannopentaose was observed. All the OAAH proteins described here exhibit potent anti-HIV activity at comparable levels. Altogether, our results provide structural details of the protein-carbohydrate interaction for this novel lectin family and insights into the molecular basis of their HIV inactivation properties. Structural Insights into the Anti-HIV Activity of the Oscillatoria agardhii Agglutinin Homolog Lectin Family.,Koharudin LM, Kollipara S, Aiken C, Gronenborn AM J Biol Chem. 2012 Sep 28;287(40):33796-811. Epub 2012 Aug 4. PMID:22865886[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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