1PHO

CRYSTAL STRUCTURES EXPLAIN FUNCTIONAL PROPERTIES OF TWO E. COLI PORINS

Summary for 1PHO

Entry DOI	10.2210/pdb1pho/pdb
Descriptor	PHOSPHOPORIN (1 entity in total)
Functional Keywords	outer membrane protein
Biological source	Escherichia coli
Cellular location	Cell outer membrane; Multi-pass membrane protein: P02932
Total number of polymer chains	1
Total formula weight	36871.25
Authors	Schirmer, T.,Cowan, S.W.,Jansonius, J.N. (deposition date: 1993-01-15, release date: 1993-10-31, Last modification date: 2024-02-14)
Primary citation	Cowan, S.W.,Schirmer, T.,Rummel, G.,Steiert, M.,Ghosh, R.,Pauptit, R.A.,Jansonius, J.N.,Rosenbusch, J.P. Crystal structures explain functional properties of two E. coli porins. Nature, 358:727-733, 1992 Cited by PubMed Abstract: Porins form aqueous channels that aid the diffusion of small hydrophilic molecules across the outer membrane of Gram-negative bacteria. The crystal structures of matrix porin and phosphoporin both reveal trimers of identical subunits, each subunit consisting of a 16-stranded anti-parallel beta-barrel containing a pore. A long loop inside the barrel contributes to a constriction of the channel where the charge distribution affects ion selectivity. The structures explain at the molecular level functional characteristics and their alterations by known mutations. PubMed: 1380671 DOI: 10.1038/358727a0 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (3 Å)

Structure validation