2X26

Crystal structure of the periplasmic aliphatic sulphonate binding protein SsuA from Escherichia coli

Summary for 2X26

• Entry DOI: 10.2210/pdb2x26/pdb
• Descriptor: PERIPLASMIC ALIPHATIC SULPHONATES-BINDING PROTEIN, GLYCEROL (3 entities in total)
• Functional Keywords: transport protein
• Biological source: ESCHERICHIA COLI
• Total number of polymer chains: 2
• Total formula weight: 67645.02

Authors

Beale, J.,Lee, S.,Iwata, S.,Beis, K. (deposition date: 2010-01-11, release date: 2010-04-14, Last modification date: 2023-12-20)

Primary citation

Beale, J.,Lee, S.Y.,Iwata, S.,Beis, K.
Structure of the Aliphatic Sulfonate-Binding Protein Ssua from Escherichia Coli
Acta Crystallogr.,Sect.F, 66:391-, 2010

PubMed 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.

PubMed: 20383006
DOI: 10.1107/S1744309110006226

Experimental method

X-RAY DIFFRACTION (1.75 Å)