5khs | pdb_00005khs

Crystal structures of the Burkholderia multivorans hopanoid transporter HpnN

spinqualitylabelsall models 5khs, resolution 3.76Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5khs is a 2 chain structure with sequence from Burkholderia multivorans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.758Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function HPNN_BURM1 Essential for hopanoid transport from the cytoplasmic to the outer membrane (PubMed:28584102). Is capable of shuttling hopanoid lipids from the inner membrane to the periplasm, where they probably spontaneously insert to the inner leaflet of the outer membrane, strengthening the cell envelope (PubMed:28584102). May be a proton-motive-force (PMF)-dependent transporter (PubMed:28584102). Is critical for multidrug resistance and cell wall remodeling in Burkholderia (PubMed:28584102). Publication Abstract from PubMed Strains of the Burkholderia cepacia 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 beta-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 hpnN gene of B. multivorans 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 B. multivorans 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 Burkholderia. Crystal structures of the Burkholderia multivorans hopanoid transporter HpnN.,Kumar N, Su CC, Chou TH, Radhakrishnan A, Delmar JA, Rajashankar KR, Yu EW Proc Natl Acad Sci U S A. 2017 Jun 20;114(25):6557-6562. doi:, 10.1073/pnas.1619660114. Epub 2017 Jun 5. PMID:28584102 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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