2X27

Crystal structure of the outer membrane protein OprG from Pseudomonas aeruginosa

Summary for 2X27

Entry DOI	10.2210/pdb2x27/pdb
Descriptor	OUTER MEMBRANE PROTEIN OPRG, NICKEL (II) ION, (HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE, ... (4 entities in total)
Functional Keywords	membrane protein, beta barrel, channel
Biological source	PSEUDOMONAS AERUGINOSA
Total number of polymer chains	1
Total formula weight	26988.28
Authors	Touw, D.S.,Patel, D.R.,van den Berg, B. (deposition date: 2010-01-11, release date: 2010-12-15, Last modification date: 2023-12-20)
Primary citation	Touw, D.S.,Patel, D.R.,van den Berg, B. The Crystal Structure of Oprg from Pseudomonas Aeruginosa, a Potential Channel for Transport of Hydrophobic Molecules Across the Outer Membrane. Plos One, 5:15016-, 2010 Cited by PubMed Abstract: The outer membrane (OM) of Gram-negative bacteria provides a barrier to the passage of hydrophobic and hydrophilic compounds into the cell. The OM has embedded proteins that serve important functions in signal transduction and in the transport of molecules into the periplasm. The OmpW family of OM proteins, of which P. aeruginosa OprG is a member, is widespread in Gram-negative bacteria. The biological functions of OprG and other OmpW family members are still unclear. PubMed: 21124774 DOI: 10.1371/JOURNAL.PONE.0015016 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.4 Å)

Structure validation