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Structural Analysis of Escherichia coli OpgG, a Protein Required for the Biosynthesis of Osmoregulated Periplasmic Glucans

2004; Elsevier BV; Volume: 342; Issue: 1 Linguagem: Inglês

10.1016/j.jmb.2004.07.004

1089-8638

Xavier Hanoulle, Églantine Rollet, Bernard Clantin, Isabelle Landrieu, Carmen Ödberg-Ferragut, Guy Lippens, Jean‐Pierre Bohin, Vincent Villeret,

Bacterial biofilms and quorum sensing

Osmoregulated periplasmic glucans (OPGs) G protein (OpgG) is required for OPGs biosynthesis. OPGs from Escherichia coli are branched glucans, with a backbone of β-1,2 glucose units and with branches attached by β-1,6 linkages. In Proteobacteria, OPGs are involved in osmoprotection, biofilm formation, virulence and resistance to antibiotics. Despite their important biological implications, enzymes synthesizing OPGs are poorly characterized. Here, we report the 2.5 Å crystal structure of OpgG from E. coli. The structure was solved using a selenemethionine derivative of OpgG and the multiple anomalous diffraction method (MAD). The protein is composed of two β-sandwich domains connected by one turn of 310 helix. The N-terminal domain (residues 22–388) displays a 25-stranded β-sandwich fold found in several carbohydrate-related proteins. It exhibits a large cleft comprising many aromatic and acidic residues. This putative binding site shares some similarities with enzymes such as galactose mutarotase and glucodextranase, suggesting a potential catalytic role for this domain in OPG synthesis. On the other hand, the C-terminal domain (residues 401–512) has a seven-stranded immunoglobulin-like β-sandwich fold, found in many proteins where it is mainly implicated in interactions with other molecules. The structural data suggest that OpgG is an OPG branching enzyme in which the catalytic activity is located in the large N-terminal domain and controlled via the smaller C-terminal domain.