title: Crystallographic and microcalorimetric analyses reveal the structural basis for high arginine specificity in the Salmonella enterica serovar Typhimurium periplasmic binding protein STM4351.
authors.affiliation: Division of Structural Biology, The Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford OX3 7BN, United Kingdom.
authors.forename: Anna L
authors.initials: AL
authors.lastname: Stamp
authors.forename: Paul
authors.initials: P
authors.lastname: Owen
authors.forename: Kamel
authors.initials: K
authors.lastname: El Omari
authors.forename: Michael
authors.initials: M
authors.lastname: Lockyer
authors.forename: Heather K
authors.initials: HK
authors.lastname: Lamb
authors.forename: Ian G
authors.initials: IG
authors.lastname: Charles
authors.forename: Alastair R
authors.initials: AR
authors.lastname: Hawkins
authors.forename: David K
authors.initials: DK
authors.lastname: Stammers
mesh_terms: D000595:Amino Acid Sequence; D001120:Arginine / Q000737:chemistry* / Q000378:metabolism; D002151:Calorimetry; D018360:Crystallography, X-Ray; D008969:Molecular Sequence Data; D033902:Periplasmic Binding Proteins / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding; D012485:Salmonella typhi / Q000737:chemistry* / Q000378:metabolism; D016415:Sequence Alignment
chemical_list: D033902:Periplasmic Binding Proteins; D001120:Arginine