1pbp: Difference between revisions

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[[Image:1pbp.jpg|left|200px]]
[[Image:1pbp.jpg|left|200px]]


{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pbp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pbp OCA], [http://www.ebi.ac.uk/pdbsum/1pbp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1pbp RCSB]</span>
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'''FINE TUNING OF THE SPECIFICITY OF THE PERIPLASMIC PHOSPHATE TRANSPORT RECEPTOR: SITE-DIRECTED MUTAGENESIS, LIGAND BINDING, AND CRYSTALLOGRAPHIC STUDIES'''
'''FINE TUNING OF THE SPECIFICITY OF THE PERIPLASMIC PHOSPHATE TRANSPORT RECEPTOR: SITE-DIRECTED MUTAGENESIS, LIGAND BINDING, AND CRYSTALLOGRAPHIC STUDIES'''
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[[Category: Quiocho, F A.]]
[[Category: Quiocho, F A.]]
[[Category: Wang, Z.]]
[[Category: Wang, Z.]]
[[Category: phosphate transport]]
[[Category: Phosphate transport]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 04:54:52 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:57:32 2008''

Revision as of 04:54, 3 May 2008

File:1pbp.jpg

Template:STRUCTURE 1pbp

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


OverviewOverview

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.

About this StructureAbout this Structure

1PBP is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Fine tuning the specificity of the periplasmic phosphate transport receptor. Site-directed mutagenesis, ligand binding, and crystallographic studies., Wang Z, Choudhary A, Ledvina PS, Quiocho FA, J Biol Chem. 1994 Oct 7;269(40):25091-4. PMID:7929197 Page seeded by OCA on Sat May 3 04:54:52 2008

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