5KHN
Crystal structures of the Burkholderia multivorans hopanoid transporter HpnN
Summary for 5KHN
| Entry DOI | 10.2210/pdb5khn/pdb |
| Related | 5KHS |
| Descriptor | RND transporter (1 entity in total) |
| Functional Keywords | transmembrane helices, membrane protein |
| Biological source | Burkholderia multivorans |
| Total number of polymer chains | 2 |
| Total formula weight | 187002.95 |
| Authors | |
| Primary citation | Kumar, 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: 28584102DOI: 10.1073/pnas.1619660114 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.445 Å) |
Structure validation
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