Structures of OppA and PstS from Yersinia pestis indicate variability of interactions with transmembrane domains

TY - JOUR

T1 - Structures of OppA and PstS from Yersinia pestis indicate variability of interactions with transmembrane domains

AU - Tanabe, Mikio

AU - Mirza, Osman

AU - Bertrand, Thomas

AU - Atkins, Helen S

AU - Titball, Richard W

AU - Iwata, So

AU - Brown, Katherine A

AU - Byrne, Bernadette

N1 - Keywords: ATP-Binding Cassette Transporters; Amino Acid Sequence; Bacterial Proteins; Binding Sites; Carrier Proteins; Crystallization; Crystallography, X-Ray; Hydrogen Bonding; Lipoproteins; Models, Molecular; Molecular Sequence Data; Periplasmic Binding Proteins; Phosphate-Binding Proteins; Protein Conformation; Protein Structure, Tertiary; Sequence Homology, Amino Acid; Yersinia pestis

PY - 2007

Y1 - 2007

N2 - Bacterial ATP-binding cassette (ABC) transport systems couple ATP hydrolysis with the uptake and efflux of a wide range of substances across bacterial membranes. These systems are comprised of transmembrane domains, nucleotide binding domains and, in the case of uptake systems, periplasmic binding proteins responsible for binding and presentation of substrate to the transmembrane domains. In pathogenic bacteria, ABC systems are known to play roles in virulence and pathogenicity and the surface localization of some components has made them attractive targets for both vaccine and anti-infective development. Here, the crystallization of five proteins (OppA, PstS, PiuA, YrbD and CysP) from Yersinia pestis, the causative agent of plague, are reported that diffracted to resolution limits ranging from 1.6 to 5 A. The first crystal structures of ABC system components from Y. pestis, OppA and PstS, are also reported here as complexes with their substrates. Comparisons of these two structures with known structures of related proteins suggest that these proteins possess versatility in substrate recognition and variations in protein-protein interactions with their cognate transmembrane domains.

AB - Bacterial ATP-binding cassette (ABC) transport systems couple ATP hydrolysis with the uptake and efflux of a wide range of substances across bacterial membranes. These systems are comprised of transmembrane domains, nucleotide binding domains and, in the case of uptake systems, periplasmic binding proteins responsible for binding and presentation of substrate to the transmembrane domains. In pathogenic bacteria, ABC systems are known to play roles in virulence and pathogenicity and the surface localization of some components has made them attractive targets for both vaccine and anti-infective development. Here, the crystallization of five proteins (OppA, PstS, PiuA, YrbD and CysP) from Yersinia pestis, the causative agent of plague, are reported that diffracted to resolution limits ranging from 1.6 to 5 A. The first crystal structures of ABC system components from Y. pestis, OppA and PstS, are also reported here as complexes with their substrates. Comparisons of these two structures with known structures of related proteins suggest that these proteins possess versatility in substrate recognition and variations in protein-protein interactions with their cognate transmembrane domains.

KW - Former Faculty of Pharmaceutical Sciences

U2 - 10.1107/S0907444907048299

DO - 10.1107/S0907444907048299

M3 - Journal article

C2 - 18007034

SN - 2059-7983

VL - 63

SP - 1185

EP - 1193

JO - Acta Crystallographica Section D: Structural Biology

JF - Acta Crystallographica Section D: Structural Biology

IS - 11

ER -