Abstract

The structure of phosphate-binding protein at 1.7 w resolution was solved and published in 1990 (Luecke & Quiocho, Nature 347, 402-406). With the recently installed 2q extension of the MAR scanner at beamline 7-1 we have collected ultra-high resolution data to 1.02 w for phosphate-binding protein from one frozen native and one frozen single-site mutant (T141D) mutant. We are in the process of refining the data with the program SHELXL (Sheldrick, G_ttingen). Initial F o-Fc maps show peaks at the positions where many of the hydrogens in the active site are expected. We hope to be able to resolve the protonation state of the bound inorganic phosphate. The phosphate is bound by 12 hydrogen bonds. There are no solvent molecules within 8 w of the completely sequestered phosphate anion. The current R-factor is 14% for all data to 1.02 w, the RFREE is 18.7%.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR001209-17
Application #
5222641
Study Section
Project Start
Project End
Budget Start
Budget End
Support Year
17
Fiscal Year
1996
Total Cost
Indirect Cost

  Publications

Vickers, Chelsea; Liu, Feng; Abe, Kento et al. (2018) Endo-fucoidan hydrolases from glycoside hydrolase family 107 (GH107) display structural and mechanistic similarities to ?-l-fucosidases from GH29. J Biol Chem 293:18296-18308
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Pluvinage, Benjamin; Grondin, Julie M; Amundsen, Carolyn et al. (2018) Molecular basis of an agarose metabolic pathway acquired by a human intestinal symbiont. Nat Commun 9:1043
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Yoshizawa, Takuya; Ali, Rustam; Jiou, Jenny et al. (2018) Nuclear Import Receptor Inhibits Phase Separation of FUS through Binding to Multiple Sites. Cell 173:693-705.e22
Feinberg, Hadar; Jégouzo, Sabine A F; Rex, Maximus J et al. (2017) Mechanism of pathogen recognition by human dectin-2. J Biol Chem 292:13402-13414
Warelow, Thomas P; Pushie, M Jake; Cotelesage, Julien J H et al. (2017) The active site structure and catalytic mechanism of arsenite oxidase. Sci Rep 7:1757

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