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PDBsum entry 4b0m
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Protein transport
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PDB id
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4b0m
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Contents |
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131 a.a.
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135 a.a.
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212 a.a.
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PDB id:
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| Name: |
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Protein transport
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Title:
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Complex of the caf1an usher domain, caf1m chaperone and caf1 subunit from yersinia pestis
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Structure:
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F1 capsule-anchoring protein. Chain: a. Fragment: residues 23-158. Engineered: yes. F1 capsule antigen. Chain: b. Engineered: yes. Chaperone protein caf1m. Chain: m.
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Source:
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Yersinia pestis. Organism_taxid: 632. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: star. Expression_system_variant: star
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Resolution:
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1.80Å
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R-factor:
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0.186
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R-free:
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0.237
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Authors:
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A.Dubnovitsky,X.D.Yu,A.F.Pudney,S.Macintyre,S.D.Knight,A.V.Zavialov
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Key ref:
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X.Di Yu
et al.
(2012).
Allosteric mechanism controls traffic in the chaperone/usher pathway.
Structure,
20,
1861-1871.
PubMed id:
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Date:
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03-Jul-12
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Release date:
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26-Sep-12
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PROCHECK
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Headers
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References
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P26949
(CAF1A_YERPE) -
F1 capsule-anchoring protein from Yersinia pestis
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Seq:
Struc:
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833 a.a.
131 a.a.
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Structure
20:1861-1871
(2012)
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PubMed id:
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Allosteric mechanism controls traffic in the chaperone/usher pathway.
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X.Di Yu,
A.Dubnovitsky,
A.F.Pudney,
S.Macintyre,
S.D.Knight,
A.V.Zavialov.
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ABSTRACT
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Many virulence organelles of Gram-negative bacterial pathogens are assembled via
the chaperone/usher pathway. The chaperone transports organelle subunits across
the periplasm to the outer membrane usher, where they are released and
incorporated into growing fibers. Here, we elucidate the mechanism of the
usher-targeting step in assembly of the Yersinia pestis F1 capsule at the atomic
level. The usher interacts almost exclusively with the chaperone in the
chaperone:subunit complex. In free chaperone, a pair of conserved proline
residues at the beginning of the subunit-binding loop form a "proline
lock" that occludes the usher-binding surface and blocks usher binding.
Binding of the subunit to the chaperone rotates the proline lock away from the
usher-binding surface, allowing the chaperone-subunit complex to bind to the
usher. We show that the proline lock exists in other chaperone/usher systems and
represents a general allosteric mechanism for selective targeting of
chaperone:subunit complexes to the usher and for release and recycling of the
free chaperone.
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Links
