2olb
From Proteopedia
(New page: 200px<br /><applet load="2olb" size="450" color="white" frame="true" align="right" spinBox="true" caption="2olb, resolution 1.4Å" /> '''OLIGOPEPTIDE BINDING ...) |
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| - | [[Image:2olb.jpg|left|200px]]<br /><applet load="2olb" size=" | + | [[Image:2olb.jpg|left|200px]]<br /><applet load="2olb" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2olb, resolution 1.4Å" /> | caption="2olb, resolution 1.4Å" /> | ||
'''OLIGOPEPTIDE BINDING PROTEIN (OPPA) COMPLEXED WITH TRI-LYSINE'''<br /> | '''OLIGOPEPTIDE BINDING PROTEIN (OPPA) COMPLEXED WITH TRI-LYSINE'''<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== | ||
| - | 2OLB 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 and ACT as [http://en.wikipedia.org/wiki/ligands ligands]. This structure | + | 2OLB 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> and <scene name='pdbligand=ACT:'>ACT</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. This structure supersedes the now removed PDB entry 1OLB. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OLB 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: ACT]] | [[Category: ACT]] | ||
[[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 18:19:46 2008'' |
Revision as of 16:19, 21 February 2008
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OLIGOPEPTIDE BINDING PROTEIN (OPPA) COMPLEXED WITH TRI-LYSINE
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
2OLB is a Single protein structure of sequence from Salmonella typhimurium with and as ligands. This structure supersedes the now removed PDB entry 1OLB. 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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