Oligopeptide-binding protein: Difference between revisions
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<StructureSection load='' size='350' side='right' caption='Oligopeptide-binding protein (grey) complex with peptide bradykinin (cyan) and Cl- ion (green) (PDB entry [[3drg]])' scene='48/488461/Cv/1'> | |||
<StructureSection load=' | |||
== Function == | == Function == | ||
'''Oligopeptide-binding protein''' (Opp) is a component of the | '''Oligopeptide-binding protein''' (Opp) is a component of the | ||
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== Structural highlights == | == Structural highlights == | ||
The bradykinin peptide is nestled between the 2 domains of Opp<ref>PMID:19300437</ref>. <scene name='48/488461/Cv/6'>Bradykinin peptide binding site</scene>. | |||
*<scene name='48/488461/Cv/7'>Cl coordination site</scene>. Water molecule is shown as red sphere. | |||
</StructureSection> | </StructureSection> | ||
==3D structures of oligopeptide-binding protein== | ==3D structures of oligopeptide-binding protein== | ||
See [[ABC transporter]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] |
Latest revision as of 10:25, 16 September 2020
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
See ABC transporter
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