title: Structure of the aliphatic sulfonate-binding protein SsuA from Escherichia coli.
abstract: Sulfur is an essential component for the biosynthesis of the sulfur-containing amino acids L-methionine and L-cysteine. Under sulfur-starvation conditions, bacteria are capable of scavenging sulfur from sulfur-containing compounds and transporting it across membranes. Here, the crystal structure of the periplasmic aliphatic sulfonate-binding protein SsuA from Escherichia coli is reported at 1.75 A resolution in the substrate-free state. The overall structure of SsuA resembles the structures of other periplasmic binding proteins and contains two globular domains that form a cleft. Comparison with other periplasmic binding proteins revealed that one of the domains has been displaced by a rigid movement of 17 degrees . Interestingly, the tight crystal packing appears to be mediated by a 13-amino-acid tail from the cloning that folds within the cleft of the next monomer.
authors.affiliation: Membrane Protein Laboratory, Diamond Light Source, Harwell Science and Innovation Campus, Oxfordshire OX11 0DE, England.
authors.forename: John
authors.initials: J
authors.lastname: Beale
authors.forename: Sang Yun
authors.initials: SY
authors.lastname: Lee
authors.forename: So
authors.initials: S
authors.lastname: Iwata
authors.forename: Konstantinos
authors.initials: K
authors.lastname: Beis
mesh_terms: D002352:Carrier Proteins / Q000737:chemistry*; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000737:chemistry*; D029968:Escherichia coli Proteins / Q000737:chemistry*; D008958:Models, Molecular; D017434:Protein Structure, Tertiary; D040681:Structural Homology, Protein
chemical_list: D002352:Carrier Proteins; D029968:Escherichia coli Proteins; C549628:SsuA protein, E coli
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