1dpe
From Proteopedia
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|PDB= 1dpe |SIZE=350|CAPTION= <scene name='initialview01'>1dpe</scene>, resolution 2.0Å | |PDB= 1dpe |SIZE=350|CAPTION= <scene name='initialview01'>1dpe</scene>, resolution 2.0Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CD:CADMIUM ION'>CD</scene> | + | |LIGAND= <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dpe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dpe OCA], [http://www.ebi.ac.uk/pdbsum/1dpe PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dpe RCSB]</span> | ||
}} | }} | ||
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[[Category: Quiocho, F A.]] | [[Category: Quiocho, F A.]] | ||
[[Category: Trakhanov, S.]] | [[Category: Trakhanov, S.]] | ||
| - | [[Category: CD]] | ||
[[Category: chemotaxis binding proteins for active transport]] | [[Category: chemotaxis binding proteins for active transport]] | ||
[[Category: peptide transport]] | [[Category: peptide transport]] | ||
[[Category: periplasmic]] | [[Category: periplasmic]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:46:02 2008'' |
Revision as of 16:46, 30 March 2008
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| , resolution 2.0Å | |||||||
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
DIPEPTIDE-BINDING PROTEIN
Overview
The family of about 50 periplasmic binding proteins, which exhibit diverse specificity (e.g., carbohydrates, amino acids, dipeptides, oligopeptides, oxyanions, metals, and vitamins) and range in size from 20 to 58 kDa, is a gold mine for an atomic-level investigation of structure and molecular recognition. These proteins serve as initial receptors for active transport systems or permeases. About six of these proteins, including the dipeptide-binding protein (DppA), are also primary receptors for chemotaxis. The structure of the unbound form of DppA (M(r) = 57,400) has been determined and refined to an R-factor of 0.169 to 2 A resolution. DppA consists of two distinct domains (I and II) connected by two "hinge" segments which form part of the base of the wide groove between the two domains. The relative orientation of the two domains gives the protein a pearlike shape, with domain I and domain II forming the larger and smaller apical ends, respectively. From the tip to the rounded bottom measures about 85 A, and the widest diameter is about 60 A. Domain I, which consists of two integrated subdomains, is folded from two separate polypeptide segments from the amino- and carboxyl-terminal ends. The more compact domain II is formed from the intervening segment. Comparison of the dipeptide-binding protein structure with that of the bound form of the similar oligopeptide-binding protein [Tame, J. R. H., Murshudov, G. N., Dodson, E. J., Neil, T. K., Dodson, G. G., Higgins, C. F., & Wilkinson, A. J. (1994) Science 264, 1578-1581] reveals the major features that differentiate the ligand specificity of the two proteins and describe the large hinge bending (about 55 degrees) between the two domains.
About this Structure
1DPE is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
2 A resolution structure of DppA, a periplasmic dipeptide transport/chemosensory receptor., Nickitenko AV, Trakhanov S, Quiocho FA, Biochemistry. 1995 Dec 26;34(51):16585-95. PMID:8527431
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