1dpp
From Proteopedia
(New page: 200px<br /><applet load="1dpp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dpp, resolution 3.2Å" /> '''DIPEPTIDE BINDING PRO...) |
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| - | [[Image:1dpp.jpg|left|200px]]<br /><applet load="1dpp" size=" | + | [[Image:1dpp.jpg|left|200px]]<br /><applet load="1dpp" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1dpp, resolution 3.2Å" /> | caption="1dpp, resolution 3.2Å" /> | ||
'''DIPEPTIDE BINDING PROTEIN COMPLEX WITH GLYCYL-L-LEUCINE'''<br /> | '''DIPEPTIDE BINDING PROTEIN COMPLEX WITH GLYCYL-L-LEUCINE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The Escherichia coli periplasmic dipeptide binding protein functions in | + | The Escherichia coli periplasmic dipeptide binding protein functions in both peptide transport and taxis toward peptides. The structure of the dipeptide binding protein in complex with Gly-Leu (glycyl-L-leucine) has been determined at 3.2 A resolution. The binding site for dipeptides is designed to recognize the ligand's backbone while providing space to accommodate a variety of side chains. Some repositioning of protein side chains lining the binding site must occur when the dipeptide's second residue is larger than leucine. The protein's fold is very similar to that of the Salmonella typhimurium oligopeptide binding protein, and a comparison of the structures reveals the structural basis for the dipeptide binding protein's preference for shorter peptides. |
==About this Structure== | ==About this Structure== | ||
| - | 1DPP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http:// | + | 1DPP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DPP OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Dunten, P.]] | [[Category: Dunten, P.]] | ||
| - | [[Category: Mowbray, S | + | [[Category: Mowbray, S L.]] |
[[Category: chemotaxis]] | [[Category: chemotaxis]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:19:07 2008'' |
Revision as of 10:19, 21 February 2008
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DIPEPTIDE BINDING PROTEIN COMPLEX WITH GLYCYL-L-LEUCINE
Overview
The Escherichia coli periplasmic dipeptide binding protein functions in both peptide transport and taxis toward peptides. The structure of the dipeptide binding protein in complex with Gly-Leu (glycyl-L-leucine) has been determined at 3.2 A resolution. The binding site for dipeptides is designed to recognize the ligand's backbone while providing space to accommodate a variety of side chains. Some repositioning of protein side chains lining the binding site must occur when the dipeptide's second residue is larger than leucine. The protein's fold is very similar to that of the Salmonella typhimurium oligopeptide binding protein, and a comparison of the structures reveals the structural basis for the dipeptide binding protein's preference for shorter peptides.
About this Structure
1DPP is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal structure of the dipeptide binding protein from Escherichia coli involved in active transport and chemotaxis., Dunten P, Mowbray SL, Protein Sci. 1995 Nov;4(11):2327-34. PMID:8563629
Page seeded by OCA on Thu Feb 21 12:19:07 2008
