Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1PBP

FINE TUNING OF THE SPECIFICITY OF THE PERIPLASMIC PHOSPHATE TRANSPORT RECEPTOR: SITE-DIRECTED MUTAGENESIS, LIGAND BINDING, AND CRYSTALLOGRAPHIC STUDIES

Summary for 1PBP
Entry DOI10.2210/pdb1pbp/pdb
DescriptorPHOSPHATE-BINDING PROTEIN, PHOSPHATE ION (3 entities in total)
Functional Keywordsphosphate transport
Biological sourceEscherichia coli
Cellular locationPeriplasm: P06128
Total number of polymer chains1
Total formula weight34566.55
Authors
Wang, Z.,Choudhary, A.,Ledvina, P.S.,Quiocho, F.A. (deposition date: 1994-07-20, release date: 1994-10-15, Last modification date: 2024-02-14)
Primary citationWang, Z.,Choudhary, A.,Ledvina, P.S.,Quiocho, F.A.
Fine tuning the specificity of the periplasmic phosphate transport receptor. Site-directed mutagenesis, ligand binding, and crystallographic studies.
J.Biol.Chem., 269:25091-25094, 1994
Cited by
PubMed Abstract: Phosphorous, primarily in the form of phosphate, is a critical nutrient for the life of a cell. We have previously determined the 1.7-A resolution structure of the phosphate-binding protein, an initial receptor for the high-affinity phosphate active transport system or permease in Escherichia coli (Luecke, H., and Quiocho, F.A. (1990) Nature 347, 402-406). This structure is the first to reveal the key role of hydrogen bonding interactions in conferring the high specificity of the permease, a specificity also shared by other phosphate transport systems. Both monobasic and dibasic phosphates are recognized by the phosphate-binding protein with Asp56 playing a key role. Here we report site-directed mutagenesis, ligand binding, and crystallographic studies of the binding protein which show that introduction of one additional Asp by mutagenesis of the Thr141 in the ligand-binding site restricts binding to only the monobasic phosphate.
PubMed: 7929197
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.9 Å)
Structure validation

238582

数据于2025-07-09公开中

PDB statisticsPDBj update infoContact PDBjnumon