1pbp: Difference between revisions

Revision as of 15:27, 21 February 2008

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 with as ligand. 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 Thu Feb 21 14:27:11 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1pbp.jpg|left|200px]]<br /><applet load="1pbp" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1pbp.jpg|left|200px]]<br /><applet load="1pbp" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1pbp, resolution 1.9&Aring;" />
 '''FINE TUNING OF THE SPECIFICITY OF THE PERIPLASMIC PHOSPHATE TRANSPORT RECEPTOR: SITE-DIRECTED MUTAGENESIS, LIGAND BINDING, AND CRYSTALLOGRAPHIC STUDIES'''<br />
 ==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.
+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==
-PBP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with PO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PBP OCA].
+PBP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=PO4:'>PO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PBP OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Choudhary, A.]]
-[[Category: Ledvina, P.S.]]
+[[Category: Ledvina, P S.]]
-[[Category: Quiocho, F.A.]]
+[[Category: Quiocho, F A.]]
 [[Category: Wang, Z.]]
 [[Category: PO4]]
 [[Category: phosphate transport]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:40:13 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:27:11 2008''