1dpp
From Proteopedia
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| - | [[Image:1dpp.jpg|left|200px]] | + | [[Image:1dpp.jpg|left|200px]] |
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| - | '''DIPEPTIDE BINDING PROTEIN COMPLEX WITH GLYCYL-L-LEUCINE''' | + | {{Structure |
| + | |PDB= 1dpp |SIZE=350|CAPTION= <scene name='initialview01'>1dpp</scene>, resolution 3.2Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''DIPEPTIDE BINDING PROTEIN COMPLEX WITH GLYCYL-L-LEUCINE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1DPP is a [ | + | 1DPP is a [[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== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8563629 8563629] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: chemotaxis]] | [[Category: chemotaxis]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:42:22 2008'' |
Revision as of 08:42, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Mar 20 10:42:22 2008
