2DVZ

Structure of a periplasmic transporter

Summary for 2DVZ

• Entry DOI: 10.2210/pdb2dvz/pdb
• Related: 2F5X
• Descriptor: Putative exported protein, CADMIUM ION, GLUTAMIC ACID, ... (4 entities in total)
• Functional Keywords: periplamsic binding proteins, carboxylate binding, glutamate, bordetella, transport protein
• Biological source: Bordetella pertussis
• Total number of polymer chains: 1
• Total formula weight: 34651.59

Authors

Huvent, I.,Belrhali, H.,Antoine, R.,Bompard, C.,Locht, C.,Jacob-Dubuisson, F.,Villeret, V. (deposition date: 2006-08-01, release date: 2006-11-07, Last modification date: 2024-10-30)

Primary citation

Huvent, I.,Belrhali, H.,Antoine, R.,Bompard, C.,Locht, C.,Jacob-Dubuisson, F.,Villeret, V.
Structural analysis of Bordetella pertussis BugE solute receptor in a bound conformation
ACTA CRYSTALLOGR.,SECT.D, 62:1375-1381, 2006

PubMed 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.

PubMed: 17057341
DOI: 10.1107/S0907444906032653

Experimental method

X-RAY DIFFRACTION (2.3 Å)