1olc
From Proteopedia
(New page: 200px<br /><applet load="1olc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1olc, resolution 2.1Å" /> '''OLIGO-PEPTIDE BINDING...) |
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| - | [[Image:1olc.gif|left|200px]]<br /><applet load="1olc" size=" | + | [[Image:1olc.gif|left|200px]]<br /><applet load="1olc" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1olc, resolution 2.1Å" /> | caption="1olc, resolution 2.1Å" /> | ||
'''OLIGO-PEPTIDE BINDING PROTEIN (OPPA) COMPLEXED WITH LYS-LYS-LYS-ALA'''<br /> | '''OLIGO-PEPTIDE BINDING PROTEIN (OPPA) COMPLEXED WITH LYS-LYS-LYS-ALA'''<br /> | ||
==Overview== | ==Overview== | ||
| - | BACKGROUND: The periplasmic oligopeptide-binding protein OppA has a | + | BACKGROUND: The periplasmic oligopeptide-binding protein OppA has a remarkably broad substrate specificity, binding peptides of two or five amino-acid residues with high affinity, but little regard to sequence. It is therefore an ideal system for studying how different chemical groups can be accommodated in a protein interior. The ability of the protein to bind peptides of different lengths has been studied by co-crystallising it with different ligands. RESULTS: Crystals of OppA from Salmonella typhimurium complexed with the peptides Lys-Lys-Lys (KKK) and Lys-Lys-Lys-Ala (KKKA) have been grown in the presence of uranyl ions which form important crystal contacts. These structures have been refined to 1.4 A and 2.1 A, respectively. The ligands are completely enclosed, their side chains pointing into large hydrated cavities and making few strong interactions with the protein. CONCLUSIONS: Tight peptide binding by OppA arises from strong hydrogen bonding and electrostatic interactions between the protein and the main chain of the ligand. Different basic side chains on the protein form salt bridges with the C terminus of peptide ligands of different lengths. |
==About this Structure== | ==About this Structure== | ||
| - | 1OLC 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 IUM as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1OLC 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=IUM:'>IUM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OLC OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Tame, J.]] | [[Category: Tame, J.]] | ||
| - | [[Category: Wilkinson, A | + | [[Category: Wilkinson, A J.]] |
[[Category: IUM]] | [[Category: IUM]] | ||
[[Category: periplasmic]] | [[Category: periplasmic]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:18:58 2008'' |
Revision as of 12:18, 21 February 2008
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OLIGO-PEPTIDE BINDING PROTEIN (OPPA) COMPLEXED WITH LYS-LYS-LYS-ALA
Overview
BACKGROUND: The periplasmic oligopeptide-binding protein OppA has a remarkably broad substrate specificity, binding peptides of two or five amino-acid residues with high affinity, but little regard to sequence. It is therefore an ideal system for studying how different chemical groups can be accommodated in a protein interior. The ability of the protein to bind peptides of different lengths has been studied by co-crystallising it with different ligands. RESULTS: Crystals of OppA from Salmonella typhimurium complexed with the peptides Lys-Lys-Lys (KKK) and Lys-Lys-Lys-Ala (KKKA) have been grown in the presence of uranyl ions which form important crystal contacts. These structures have been refined to 1.4 A and 2.1 A, respectively. The ligands are completely enclosed, their side chains pointing into large hydrated cavities and making few strong interactions with the protein. CONCLUSIONS: Tight peptide binding by OppA arises from strong hydrogen bonding and electrostatic interactions between the protein and the main chain of the ligand. Different basic side chains on the protein form salt bridges with the C terminus of peptide ligands of different lengths.
About this Structure
1OLC is a Single protein structure of sequence from Salmonella typhimurium with as ligand. Full crystallographic information is available from OCA.
Reference
The crystal structures of the oligopeptide-binding protein OppA complexed with tripeptide and tetrapeptide ligands., Tame JR, Dodson EJ, Murshudov G, Higgins CF, Wilkinson AJ, Structure. 1995 Dec 15;3(12):1395-406. PMID:8747465
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