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3JTY

Crystal structure of a BenF-like porin from Pseudomonas fluorescens Pf-5

Summary for 3JTY
Entry DOI10.2210/pdb3jty/pdb
DescriptorBenF-like porin, LAURYL DIMETHYLAMINE-N-OXIDE (3 entities in total)
Functional Keywordspfl_1329, benf-like porin, pseudomonas fluorescens pf-5, benzoate transporter, efflux pump, structural genomics, psi-2, protein structure initiative, new york structural genomix research consortium, nysgxrc, new york sgx research center for structural genomics, transport protein
Biological sourcePseudomonas fluorescens Pf-5
Total number of polymer chains4
Total formula weight179416.90
Authors
Primary citationSampathkumar, P.,Lu, F.,Zhao, X.,Li, Z.,Gilmore, J.,Bain, K.,Rutter, M.E.,Gheyi, T.,Schwinn, K.D.,Bonanno, J.B.,Pieper, U.,Fajardo, J.E.,Fiser, A.,Almo, S.C.,Swaminathan, S.,Chance, M.R.,Baker, D.,Atwell, S.,Thompson, D.A.,Emtage, J.S.,Wasserman, S.R.,Sali, A.,Sauder, J.M.,Burley, S.K.
Structure of a putative BenF-like porin from Pseudomonas fluorescens Pf-5 at 2.6 A resolution.
Proteins, 78:3056-3062, 2010
Cited by
PubMed Abstract: The X-ray structure of a putative BenF-like (gene name: PFL1329) protein from (PflBenF) has been determined at 2.6Å resolution. X-ray crystallography revealed a canonical 18-stranded β-barrel fold that forms a central pore with a diameter of ∼4.6Å, which is consistent with the size and physicochemical properties of the presumed aromatic acid substrate, benzoate. Detailed comparisons with the previously-determined structure of OpdK, a vanillate influx channel, revealed an arginine-rich aromatic acid selectivity filter of nearly identical structure composed of seven highly conserved residues Arg∼Asp∼Arg∼Arg∼Ser∼Asp∼Arg (R∼D∼R∼R∼S∼D∼R sequence motif, where ∼ denotes intervening residues) that define the narrowest part of the pore.
PubMed: 20737437
DOI: 10.1002/prot.22829
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.58 Å)
Structure validation

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