PDBsum entry 4fbv

Carbohydrate binding protein

PDB id: 4fbv

Contents

Protein chain

266 a.a.

Ligands

BMA-MAN-MAN-MAN

BMA-MAN-MAN-MAN-MAN

MAN

EDO ×4

Waters ×197

PDB id:

4fbv

Name:

Carbohydrate binding protein

Title:

Crystal structure of the myxococcus xanthus hemagglutinin in complex with a3,a6-mannopentaose

Structure:

Myxobacterial hemagglutinin. Chain: a. Synonym: lectin. Engineered: yes

Source:

Myxococcus xanthus. Organism_taxid: 34. Gene: mbha. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.76Å R-factor: 0.188 R-free: 0.214

Authors:

L.M.I.Koharudin,A.M.Gronenborn

Key ref:

L.M.Koharudin et al. (2012). Structural insights into the anti-HIV activity of the Oscillatoria agardhii agglutinin homolog lectin family. J Biol Chem, 287, 33796-33811. PubMed id: 22865886

Date:

23-May-12 Release date: 15-Aug-12

Protein chain

P07386  (MBHA_MYXXA) -  Myxobacterial hemagglutinin from Myxococcus xanthus

Seq: 267 a.a.

Struc: 266 a.a.

J Biol Chem 287:33796-33811 (2012)

PubMed id: 22865886

Structural insights into the anti-HIV activity of the Oscillatoria agardhii agglutinin homolog lectin family.

L.M.Koharudin, S.Kollipara, C.Aiken, A.M.Gronenborn.

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.