Oligopeptide-binding protein: Difference between revisions
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**[[3tcf]], [[3tcg]], [[3tch]] - OPP + peptide – ''Escherichia coli''<br /> | **[[3tcf]], [[3tcg]], [[3tch]] - OPP + peptide – ''Escherichia coli''<br /> | ||
**[[3zs6]] - OPP + peptide – ''Burkholderia pseudomallei''<br /> | **[[3zs6]] - OPP + peptide – ''Burkholderia pseudomallei''<br /> | ||
**[[6dqq]], [[6dqr]], [[6dqt]], [[6dqu]], [[6dtf]], [[6dtg]], [[6dth]] - OPP + peptide – ''Haemophilus influenzae''<br /> | |||
}} | }} | ||
== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Revision as of 13:25, 12 November 2019
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 12-November-2019
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