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1dpp

From Proteopedia

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[[Image:1dpp.jpg|left|200px]]
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{{STRUCTURE_1dpp| PDB=1dpp | SCENE= }}
{{STRUCTURE_1dpp| PDB=1dpp | SCENE= }}
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'''DIPEPTIDE BINDING PROTEIN COMPLEX WITH GLYCYL-L-LEUCINE'''
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===DIPEPTIDE BINDING PROTEIN COMPLEX WITH GLYCYL-L-LEUCINE===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 8563629 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8563629}}
==About this Structure==
==About this Structure==
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[[Category: Mowbray, S L.]]
[[Category: Mowbray, S L.]]
[[Category: Chemotaxis]]
[[Category: Chemotaxis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 30 13:52:43 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:25:47 2008''

Revision as of 20:25, 30 June 2008

Image:1dpp.png

Template:STRUCTURE 1dpp

DIPEPTIDE BINDING PROTEIN COMPLEX WITH GLYCYL-L-LEUCINE

Template:ABSTRACT PUBMED 8563629

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 Mon Jun 30 23:25:47 2008

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