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PDBsum entry 6tfs
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Transport protein
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PDB id
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6tfs
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PDB id:
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| Name: |
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Transport protein
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Title:
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Structure in p3212 form of the pbp/sbp moaa in complex with glucopinic acid from a.Tumefacien r10
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Structure:
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Abc transporter substrate-binding protein. Chain: a, b. Synonym: moaa,peptide/nickel transport system substrate-binding protein,polyamine abc transporter substrate-binding protein. Engineered: yes
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Source:
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Rhizobium radiobacter. Agrobacterium tumefaciens. Organism_taxid: 358. Gene: moaa, ddpa, a6u90_18755, at1d1609_52430, ata6_55190. Expressed in: escherichia coli. Expression_system_taxid: 562
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Resolution:
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2.00Å
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R-factor:
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0.184
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R-free:
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0.194
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Authors:
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S.Morera,A.Vigouroux
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Key ref:
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A.Vigouroux
et al.
(2020).
Import pathways of the mannityl-opines into the bacterial pathogen Agrobacterium tumefaciens: structural, affinity and in vivo approaches.
Biochem J,
477,
615-628.
PubMed id:
DOI:
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Date:
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14-Nov-19
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Release date:
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22-Jan-20
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PROCHECK
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Headers
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References
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O50271
(O50271_RHIRD) -
ABC transporter substrate-binding protein from Rhizobium radiobacter
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Seq:
Struc:
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522 a.a.
493 a.a.
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DOI no:
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Biochem J
477:615-628
(2020)
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PubMed id:
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Import pathways of the mannityl-opines into the bacterial pathogen Agrobacterium tumefaciens: structural, affinity and in vivo approaches.
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A.Vigouroux,
J.Doré,
L.Marty,
M.Aumont-Nicaise,
P.Legrand,
Y.Dessaux,
L.Vial,
S.Moréra.
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ABSTRACT
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Agrobacterium tumefaciens pathogens use specific compounds denoted opines as
nutrients in their plant tumor niche. These opines are produced by the host
plant cells genetically modified by agrobacteria. They are imported into
bacteria via solute-binding proteins (SBPs) in association with ATP-binding
cassette transporters. The mannityl-opine family encompasses mannopine,
mannopinic acid, agropine and agropinic acid. Structural and affinity data on
mannopinic acid bound to SBPs are currently lacking while those of the three
others mannityl opines are available. We investigated the molecular basis of two
pathways for mannopinic acid uptake. MoaA was proposed as the specific SBP for
mannopinic acid import in mannityl opines-assimilating agrobacteria, which was
validated here using genetic studies and affinity measurements. We structurally
characterized the mannopinic acid-binding mode of MoaA in two crystal forms at
2.05 and 1.57 Å resolution. We demonstrated that the non-specific SBP MotA,
so far characterized as mannopine and Amadori compound importer, was also able
to transport mannopinic acid. The structure of MotA bound to mannopinic acid at
2.2 Å resolution defines a different mannopinic acid-binding signature,
similar to that of mannopine. Combining in vitro and in vivo approaches, this
work allowed us to complete the characterization of the mannityl-opines
assimilation pathways, highlighting the important role of two dual imports of
agropinic and mannopinic acids. Our data shed new light on how the
mannityl-opines contribute to the establishment of the ecological niche of
agrobacteria from the early to the late stages of tumor development.
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Links
