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Structural analysis ofBordetella pertussisBugE solute receptor in a bound conformation
- Source :
- Acta Crystallographica Section D Biological Crystallography. 62:1375-1381
- Publication Year :
- 2006
- Publisher :
- International Union of Crystallography (IUCr), 2006.
-
Abstract
- The Bug proteins form a large family of periplasmic solute-binding receptors present in a number of bacterial species. Here, the crystal structure of Bordetella pertussis BugE, a member of the Bug family coded by the gene BP0250, is reported. It adopts the Venus flytrap architecture of periplasmic binding proteins, with two domains separated by a deep cleft. BugE has a bound ligand, identified as a glutamate. The structure of B. pertussis BugD, which is an aspartic acid transporter, has recently been reported. These structures reveal high conservation of the Bug architecture, despite limited sequence identity. They share a common carboxylate-binding motif defined by two strand-beta-turn-alpha-helix motifs, also involving two water molecules to bridge the carboxylate O atoms to the protein. The two water molecules are hydrogen bonded to a common main-chain carbonyl group. Although the features of the carboxylate-binding motif are totally conserved, the ligand in BugE is bound by its side-chain carboxylate group rather than by its alpha-carboxylate as in BugD. This specific ligand-binding motif is highly conserved in Bug proteins and the BugE structure suggests that the cavity of the Bug proteins might also accommodate carboxylated solutes other than amino acids. The vast expansion of the Bug family in several bacterial genera is likely to be explained by the possible diversity of ligands. No charged residues are involved in glutamate binding by BugE, unlike what has been described for all glutamate receptors reported so far.
- Subjects :
- chemistry.chemical_classification
Bordetella pertussis
Ligand
Amino Acid Motifs
Glutamate binding
General Medicine
Periplasmic space
Biology
Crystallography, X-Ray
Ligands
biology.organism_classification
Protein Structure, Tertiary
Transport protein
Amino acid
Biochemistry
chemistry
Structural Biology
Periplasmic Binding Proteins
Periplasm
Aspartic acid
Subjects
Details
- ISSN :
- 09074449
- Volume :
- 62
- Database :
- OpenAIRE
- Journal :
- Acta Crystallographica Section D Biological Crystallography
- Accession number :
- edsair.doi.dedup.....0ffc8bfbb75a4c7caf99513481e7ac00