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5KHS

Crystal structures of the Burkholderia multivorans hopanoid transporter HpnN

Summary for 5KHS
Entry DOI10.2210/pdb5khs/pdb
Related5KHN
DescriptorPutative RND superfamily efflux pump membrane protein (1 entity in total)
Functional Keywordstransmembrane helices, membrane protein
Biological sourceBurkholderia multivorans
Total number of polymer chains2
Total formula weight187002.95
Authors
Su, C.-C.,Yu, E.W. (deposition date: 2016-06-15, release date: 2017-06-14, Last modification date: 2024-03-06)
Primary citationKumar, N.,Su, C.C.,Chou, T.H.,Radhakrishnan, A.,Delmar, J.A.,Rajashankar, K.R.,Yu, E.W.
Crystal structures of the Burkholderia multivorans hopanoid transporter HpnN.
Proc. Natl. Acad. Sci. U.S.A., 114:6557-6562, 2017
Cited by
PubMed Abstract: Strains of the complex (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. The gene of encodes 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 of HpnN, 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 in .
PubMed: 28584102
DOI: 10.1073/pnas.1619660114
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.758 Å)
Structure validation

237735

数据于2025-06-18公开中

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