title: Importance of a hydrophobic pocket for peptide binding in lactococcal OppA.
abstract: Lactococcal oligopeptide-binding protein A (OppA) binds peptides with widely varied lengths and sequences. We previously hypothesized that a hydrophobic pocket in OppA preferentially binds a hydrophobic peptide side chain and thus determines its binding register. Two crystal structures of OppA with different nonapeptides now indeed show binding in different registers.
authors.affiliation: Biochemistry Department, Groningen Biomolecular Sciences and Biotechnology Center, NPC & Zernike Institute for Advanced Materials, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands.
authors.forename: Ronnie P-A
authors.initials: RP
authors.lastname: Berntsson
authors.forename: Andy-Mark W H
authors.initials: AM
authors.lastname: Thunnissen
authors.forename: Bert
authors.initials: B
authors.lastname: Poolman
authors.forename: Dirk-Jan
authors.initials: DJ
authors.lastname: Slotboom
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D001665:Binding Sites; D002352:Carrier Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D003460:Crystallization; D057927:Hydrophobic and Hydrophilic Interactions; D013294:Lactococcus lactis / Q000378:metabolism*; D008074:Lipoproteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation
chemical_list: D001426:Bacterial Proteins; D002352:Carrier Proteins; D008074:Lipoproteins; C046506:oligopeptide-binding protein, bacteria