1pbp
From Proteopedia
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|PDB= 1pbp |SIZE=350|CAPTION= <scene name='initialview01'>1pbp</scene>, resolution 1.9Å | |PDB= 1pbp |SIZE=350|CAPTION= <scene name='initialview01'>1pbp</scene>, resolution 1.9Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=PO4:PHOSPHATE ION'>PO4</scene> | + | |LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |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> | ||
}} | }} | ||
| Line 26: | Line 29: | ||
[[Category: Quiocho, F A.]] | [[Category: Quiocho, F A.]] | ||
[[Category: Wang, Z.]] | [[Category: Wang, Z.]] | ||
| - | [[Category: PO4]] | ||
[[Category: phosphate transport]] | [[Category: phosphate transport]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:57:32 2008'' |
Revision as of 19:57, 30 March 2008
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| , resolution 1.9Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
FINE TUNING OF THE SPECIFICITY OF THE PERIPLASMIC PHOSPHATE TRANSPORT RECEPTOR: SITE-DIRECTED MUTAGENESIS, LIGAND BINDING, AND CRYSTALLOGRAPHIC STUDIES
Overview
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 Structure
1PBP is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
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
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