4FBV
Crystal structure of the Myxococcus Xanthus hemagglutinin in complex with a3,a6-mannopentaose
Summary for 4FBV
| Entry DOI | 10.2210/pdb4fbv/pdb |
| Related | 3OBL 3S5V 4FBO 4FBR |
| Descriptor | Myxobacterial hemagglutinin, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose, ... (6 entities in total) |
| Functional Keywords | beta-barrel, hiv-inactivating, carbohydrate binding protein |
| Biological source | Myxococcus xanthus |
| Total number of polymer chains | 1 |
| Total formula weight | 29860.38 |
| Authors | Koharudin, L.M.I.,Gronenborn, A.M. (deposition date: 2012-05-23, release date: 2012-08-15, Last modification date: 2023-09-13) |
| Primary citation | Koharudin, L.M.,Kollipara, S.,Aiken, C.,Gronenborn, A.M. Structural Insights into the Anti-HIV Activity of the Oscillatoria agardhii Agglutinin Homolog Lectin Family. J.Biol.Chem., 287:33796-33811, 2012 Cited by PubMed Abstract: Oscillatoria agardhii agglutinin homolog (OAAH) proteins belong to a recently discovered lectin family. All members contain a sequence repeat of ~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 α3,α6-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. PubMed: 22865886DOI: 10.1074/jbc.M112.388579 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.76 Å) |
Structure validation
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