5I5F

Salmonella global domain 191

Summary for 5I5F

• Entry DOI: 10.2210/pdb5i5f/pdb
• Descriptor: Inner membrane protein YejM (2 entities in total)
• Functional Keywords: salmonella 191-586, membrane protein
• Biological source: Salmonella typhimurium
• Total number of polymer chains: 4
• Total formula weight: 268785.94

Authors

Dong, C.,Dong, H. (deposition date: 2016-02-15, release date: 2016-08-17, Last modification date: 2024-05-08)

Primary citation

Dong, H.,Zhang, Z.,Tang, X.,Huang, S.,Li, H.,Peng, B.,Dong, C.
Structural insights into cardiolipin transfer from the Inner membrane to the outer membrane by PbgA in Gram-negative bacteria.
Sci Rep, 6:30815-30815, 2016

PubMed Abstract: The outer membrane (OM) of Gram-negative bacteria is a unique asymmetric lipid bilayer in which the outer leaflet is composed of lipopolysaccharide (LPS) and the inner leaflet is formed by glycerophospholipid (GPL). The OM plays a fundamental role in protecting Gram-negative bacteria from harsh environments and toxic compounds. The transport and assembly pathways for phospholipids of bacterial OM are unknown. Cardiolipin (CL) plays an important role in OM biogenesis and pathogenesis, and the inner membrane (IM) protein PbgA, containing five transmembrane domains and a globular domain in periplasm has been recently identified as a CL transporter from the IM to the OM with an unknown mechanism. Here we present the first two crystal structures of soluble periplasmic globular domain of PbgA from S. typhimurium and E. coli, which revealed that the globular domains of PbgA resemble the structures of the arylsulfatase protein family and contains a novel core hydrophobic pocket that may be responsible for binding and transporting CLs. Our structural and functional studies shed an important light on the mechanism of CL transport in Gram-negative bacteria from the IM to the OM, which offers great potential for the development of novel antibiotics against multi-drug resistant bacterial infections.

PubMed: 27487745
DOI: 10.1038/srep30815

Experimental method

X-RAY DIFFRACTION (1.84 Å)