1ola
From Proteopedia
(New page: 200px<br /><applet load="1ola" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ola, resolution 2.1Å" /> '''THE STRUCTURAL BASIS ...) |
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| - | [[Image:1ola.gif|left|200px]]<br /><applet load="1ola" size=" | + | [[Image:1ola.gif|left|200px]]<br /><applet load="1ola" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ola, resolution 2.1Å" /> | caption="1ola, resolution 2.1Å" /> | ||
'''THE STRUCTURAL BASIS OF MULTISPECIFICITY IN THE OLIGOPEPTIDE-BINDING PROTEIN OPPA'''<br /> | '''THE STRUCTURAL BASIS OF MULTISPECIFICITY IN THE OLIGOPEPTIDE-BINDING PROTEIN OPPA'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Specific protein-ligand interactions are critical for cellular function, and most proteins select their partners with sharp discrimination. | + | Specific protein-ligand interactions are critical for cellular function, and most proteins select their partners with sharp discrimination. However, the oligopeptide-binding protein of Salmonella typhimurium (OppA) binds peptides of two to five amino acid residues without regard to sequence. The crystal structure of OppA reveals a three-domain organization, unlike other periplasmic binding proteins. In OppA-peptide complexes, the ligands are completely enclosed in the protein interior, a mode of binding that normally imposes tight specificity. The protein fulfills the hydrogen bonding and electrostatic potential of the ligand main chain and accommodates the peptide side chains in voluminous hydrated cavities. |
==About this Structure== | ==About this Structure== | ||
| - | 1OLA 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:// | + | 1OLA 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=1OLA 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: binding protein]] | [[Category: binding protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:19:03 2008'' |
Revision as of 12:19, 21 February 2008
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THE STRUCTURAL BASIS OF MULTISPECIFICITY IN THE OLIGOPEPTIDE-BINDING PROTEIN OPPA
Overview
Specific protein-ligand interactions are critical for cellular function, and most proteins select their partners with sharp discrimination. However, the oligopeptide-binding protein of Salmonella typhimurium (OppA) binds peptides of two to five amino acid residues without regard to sequence. The crystal structure of OppA reveals a three-domain organization, unlike other periplasmic binding proteins. In OppA-peptide complexes, the ligands are completely enclosed in the protein interior, a mode of binding that normally imposes tight specificity. The protein fulfills the hydrogen bonding and electrostatic potential of the ligand main chain and accommodates the peptide side chains in voluminous hydrated cavities.
About this Structure
1OLA is a Single protein structure of sequence from Salmonella typhimurium with as ligand. Full crystallographic information is available from OCA.
Reference
The structural basis of sequence-independent peptide binding by OppA protein., Tame JR, Murshudov GN, Dodson EJ, Neil TK, Dodson GG, Higgins CF, Wilkinson AJ, Science. 1994 Jun 10;264(5165):1578-81. PMID:8202710
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