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PDBsum entry 5khs
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Membrane protein
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PDB id
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5khs
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References listed in PDB file
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Key reference
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Title
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Crystal structures of theburkholderia multivoranshopanoid transporter hpnn.
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Authors
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N.Kumar,
C.C.Su,
T.H.Chou,
A.Radhakrishnan,
J.A.Delmar,
K.R.Rajashankar,
E.W.Yu.
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Ref.
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Proc Natl Acad Sci U S A, 2017,
114,
6557-6562.
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PubMed id
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Abstract
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Strains of theBurkholderia cepaciacomplex (Bcc) are Gram-negative
opportunisitic bacteria that are capable of causing serious diseases, mainly in
immunocompromised individuals. Bcc pathogens are intrinsically resistant to
multiple antibiotics, including β-lactams, aminoglycosides, fluoroquinolones,
and polymyxins. They are major pathogens in patients with cystic fibrosis (CF)
and can cause severe necrotizing pneumonia, which is often fatal. Hopanoid
biosynthesis is one of the major mechanisms involved in multiple antimicrobial
resistance of Bcc pathogens. ThehpnNgene ofB. multivoransencodes
an integral membrane protein of the HpnN family of transporters, which is
responsible for shuttling hopanoids to the outer membrane. Here, we report
crystal structures ofB. multivoransHpnN, revealing a dimeric molecule
with an overall butterfly shape. Each subunit of the transporter contains 12
transmembrane helices and two periplasmic loops that suggest a plausible pathway
for substrate transport. Further analyses indicate that HpnN is capable of
shuttling hopanoid virulence factors from the outer leaflet of the inner
membrane to the periplasm. Taken together, our data suggest that the HpnN
transporter is critical for multidrug resistance and cell wall remodeling
inBurkholderia.
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