6D79

Structure of CysZ, a sulfate permease from Pseudomonas Fragi

Summary for 6D79

• Entry DOI: 10.2210/pdb6d79/pdb
• Related: 3TX3
• Descriptor: Sulfate transporter CysZ (1 entity in total)
• Functional Keywords: membrane protein, sulfate translocation, prokaryotic cysteine biosynthesis, transport protein
• Biological source: Pseudomonas fragi A22
• Total number of polymer chains: 2
• Total formula weight: 57837.88

Authors

Sanghai, Z.A.,Liu, Q.,Clarke, O.B.,Banerjee, S.,Rajashankar, K.R.,Hendrickson, W.A.,Mancia, F. (deposition date: 2018-04-24, release date: 2018-05-16, Last modification date: 2024-10-16)

Primary citation

Assur Sanghai, Z.,Liu, Q.,Clarke, O.B.,Belcher-Dufrisne, M.,Wiriyasermkul, P.,Giese, M.H.,Leal-Pinto, E.,Kloss, B.,Tabuso, S.,Love, J.,Punta, M.,Banerjee, S.,Rajashankar, K.R.,Rost, B.,Logothetis, D.,Quick, M.,Hendrickson, W.A.,Mancia, F.
Structure-based analysis of CysZ-mediated cellular uptake of sulfate.
Elife, 7:-, 2018

PubMed Abstract: Sulfur, most abundantly found in the environment as sulfate (SO), is an essential element in metabolites required by all living cells, including amino acids, co-factors and vitamins. However, current understanding of the cellular delivery of SO at the molecular level is limited. CysZ has been described as a SO permease, but its sequence family is without known structural precedent. Based on crystallographic structure information, SO binding and flux experiments, we provide insight into the molecular mechanism of CysZ-mediated translocation of SO across membranes. CysZ structures from three different bacterial species display a hitherto unknown fold and have subunits organized with inverted transmembrane topology. CysZ from assembles as a trimer of antiparallel dimers and the CysZ structures from two other species recapitulate dimers from this assembly. Mutational studies highlight the functional relevance of conserved CysZ residues.

PubMed: 29792261
DOI: 10.7554/eLife.27829

Experimental method

X-RAY DIFFRACTION (3.501 Å)