Oligopeptide-binding protein: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
The bradykinin peptide is nestled between the 2 domains of Opp<ref>PMID:19300437</ref>. | The bradykinin peptide is nestled between the 2 domains of Opp<ref>PMID:19300437</ref>. <scene name='48/488461/Cv/3'>Bradykinin peptide binding site</scene>. | ||
</StructureSection> | </StructureSection> | ||
Revision as of 14:30, 8 June 2016
FunctionOligopeptide-binding protein (Opp) is a component of the oligopeptide permease which is an ABC-type transporter system. Opp binds polypeptides up to pentapeptide in length with high affinity. Opp is required for sporulation and competence. Opp carries oligopeptides to the membrane-associated oligopeptide permease[1]. Structural highlightsThe bradykinin peptide is nestled between the 2 domains of Opp[2]. . |
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3D structures of oligopeptide-binding protein3D structures of oligopeptide-binding protein
Updated on 08-June-2016
ReferencesReferences
- ↑ Monnet V. Bacterial oligopeptide-binding proteins. Cell Mol Life Sci. 2003 Oct;60(10):2100-14. PMID:14618258 doi:http://dx.doi.org/10.1007/s00018-003-3054-3
- ↑ Berntsson RP, Doeven MK, Fusetti F, Duurkens RH, Sengupta D, Marrink SJ, Thunnissen AM, Poolman B, Slotboom DJ. The structural basis for peptide selection by the transport receptor OppA. EMBO J. 2009 Mar 19. PMID:19300437 doi:emboj200965