Periplasmic dipeptide-binding protein: Difference between revisions

Periplasmic binding proteins (PBPs) are non-enzymatic receptors that bacteria use to sense small molecules such as carbohydrates, amino acids, and ions, and transport them into the cytoplasm<ref name=ACS>DOI: 10.1021/cb900021q</ref>.  These sorts of proteins are ubiquitous in both gram-negative and gram-positive bacteria, appearing in gram-positive bacteria as membrane-anchored lipoproteins<ref name=ACS/>.  The glucose/galactose binding protein (<scene name='84/842887/Gbbp/4'>GBBP</scene>) of ''E. coli'' is amongst the best studied of these proteins<ref>DOI: 10.1016/j.cbpa.2013.12.014</ref>.    These proteins typically exhibit a “Venus fly-trap” appearance, consisting of two globular domains connected by a small hinge region<ref name=ACS/>.  The hinge-like appearance is evident in GBBP.  These proteins often also work in conjunction with an ABC-binding cassette transporter which catalyzes the movement of the substance at hand across the cytoplasmic membrane.

[[6ofq]], [[6pu3]] – DppA + peptide – ''Helicobacter pylori''<br />