1laf: Difference between revisions

Revision as of 14:43, 21 February 2008

STRUCTURAL BASES FOR MULTIPLE LIGAND SPECIFICITY OF THE PERIPLASMIC LYSINE-, ARGININE-, ORNITHINE-BINDING PROTEIN

OverviewOverview

The substrate-binding site of a protein with multiple specificity should satisfy geometric and energetic complementarity for several different substrates. The structural basis of the multiple ligand specificity of the periplasmic lysine-, arginine-, ornithine-binding protein (LAO) was investigated by determining and analyzing the structures of the protein unliganded and liganded with each of the three high-affinity ligands (L-lysine, L-arginine, and L-ornithine) and with one low-affinity ligand (L-histidine). The geometric complementarity is achieved primarily by virtue of the large size of the ligand-binding site which can accommodate the maximum common volume of the four ligands plus three water molecules. The optimization of energetic complementarity is achieved by the relocation of protein-bound water molecules and by the movement of the Asp-11 side chain. The structure of the LAO-histidine complex indicates that the 30-fold reduced affinity of the protein for histidine is primarily due to unavailability of one ionic interaction of the histidine side chain with the protein which is present in the other three complexes.

About this StructureAbout this Structure

1LAF is a Single protein structure of sequence from Salmonella typhimurium with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis for multiple ligand specificity of the periplasmic lysine-, arginine-, ornithine-binding protein., Oh BH, Ames GF, Kim SH, J Biol Chem. 1994 Oct 21;269(42):26323-30. PMID:7929349

Page seeded by OCA on Thu Feb 21 13:43:04 2008

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OCA

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-[[Image:1laf.gif|left|200px]]<br /><applet load="1laf" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1laf.gif|left|200px]]<br /><applet load="1laf" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1laf, resolution 2.06&Aring;" />
 '''STRUCTURAL BASES FOR MULTIPLE LIGAND SPECIFICITY OF THE PERIPLASMIC LYSINE-, ARGININE-, ORNITHINE-BINDING PROTEIN'''<br />
 ==Overview==
-The substrate-binding site of a protein with multiple specificity should, satisfy geometric and energetic complementarity for several different, substrates. The structural basis of the multiple ligand specificity of the, periplasmic lysine-, arginine-, ornithine-binding protein (LAO) was, investigated by determining and analyzing the structures of the protein, unliganded and liganded with each of the three high-affinity ligands, (L-lysine, L-arginine, and L-ornithine) and with one low-affinity ligand, (L-histidine). The geometric complementarity is achieved primarily by, virtue of the large size of the ligand-binding site which can accommodate, the maximum common volume of the four ligands plus three water molecules., The optimization of energetic complementarity is achieved by the, relocation of protein-bound water molecules and by the movement of the, Asp-11 side chain. The structure of the LAO-histidine complex indicates, that the 30-fold reduced affinity of the protein for histidine is, primarily due to unavailability of one ionic interaction of the histidine, side chain with the protein which is present in the other three complexes.
+The substrate-binding site of a protein with multiple specificity should satisfy geometric and energetic complementarity for several different substrates. The structural basis of the multiple ligand specificity of the periplasmic lysine-, arginine-, ornithine-binding protein (LAO) was investigated by determining and analyzing the structures of the protein unliganded and liganded with each of the three high-affinity ligands (L-lysine, L-arginine, and L-ornithine) and with one low-affinity ligand (L-histidine). The geometric complementarity is achieved primarily by virtue of the large size of the ligand-binding site which can accommodate the maximum common volume of the four ligands plus three water molecules. The optimization of energetic complementarity is achieved by the relocation of protein-bound water molecules and by the movement of the Asp-11 side chain. The structure of the LAO-histidine complex indicates that the 30-fold reduced affinity of the protein for histidine is primarily due to unavailability of one ionic interaction of the histidine side chain with the protein which is present in the other three complexes.
 ==About this Structure==
-LAF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium] with ARG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LAF OCA].
+LAF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium] with <scene name='pdbligand=ARG:'>ARG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LAF OCA].
 ==Reference==
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 [[Category: Salmonella typhimurium]]
 [[Category: Single protein]]
-[[Category: Kim, S.H.]]
+[[Category: Kim, S H.]]
-[[Category: Oh, B.H.]]
+[[Category: Oh, B H.]]
 [[Category: ARG]]
 [[Category: amino acid transport]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:25:31 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:43:04 2008''