2dri: Difference between revisions
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'''PROBING PROTEIN-PROTEIN INTERACTIONS: THE RIBOSE BINDING PROTEIN IN BACTERIAL TRANSPORT AND CHEMOTAXIS''' | {{Structure | ||
|PDB= 2dri |SIZE=350|CAPTION= <scene name='initialview01'>2dri</scene>, resolution 1.6Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=RIP:RIBOSE(PYRANOSE FORM)'>RIP</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''PROBING PROTEIN-PROTEIN INTERACTIONS: THE RIBOSE BINDING PROTEIN IN BACTERIAL TRANSPORT AND CHEMOTAXIS''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2DRI is a [ | 2DRI is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry 1DRI. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DRI OCA]. | ||
==Reference== | ==Reference== | ||
Probing protein-protein interactions. The ribose-binding protein in bacterial transport and chemotaxis., Bjorkman AJ, Binnie RA, Zhang H, Cole LB, Hermodson MA, Mowbray SL, J Biol Chem. 1994 Dec 2;269(48):30206-11. PMID:[http:// | Probing protein-protein interactions. The ribose-binding protein in bacterial transport and chemotaxis., Bjorkman AJ, Binnie RA, Zhang H, Cole LB, Hermodson MA, Mowbray SL, J Biol Chem. 1994 Dec 2;269(48):30206-11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7982928 7982928] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: sugar transport]] | [[Category: sugar transport]] | ||
''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 16:30:35 2008'' | ||
Revision as of 17:30, 20 March 2008
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PROBING PROTEIN-PROTEIN INTERACTIONS: THE RIBOSE BINDING PROTEIN IN BACTERIAL TRANSPORT AND CHEMOTAXIS
OverviewOverview
A number of mutations at Gly134 of the periplasmic ribose-binding protein of Escherichia coli were examined by a combined biochemical and structural approach. Different mutations gave rise to different patterns of effects on the chemotaxis and transport functions. The smallest residue (alanine) had the least effect on transport, whereas large hydrophobic residues had the smallest effect on chemotaxis. Comparison of the x-ray crystal structure of the G134R mutant protein (2.5-A resolution) to that of the wild type (1.6-A resolution) showed that the basic structure of the protein was unaltered. The loss of chemotaxis and transport functions in this and similar mutant proteins must therefore be caused by relatively simple surface effects, which include a change in local main chain conformation. The loss of chemotaxis and transport functions resulting from the introduction of an alanine residue at position 134 was suppressed by an additional isoleucine to threonine mutation at residue 132. An x-ray structure of the I132T/G134A double mutant protein (2.2-A resolution) showed that the changes in local structure were accompanied by a diffuse pattern of structural changes in the surrounding region, implying that the suppression derives from a combination of sources.
About this StructureAbout this Structure
2DRI is a Single protein structure of sequence from Escherichia coli. This structure supersedes the now removed PDB entry 1DRI. Full crystallographic information is available from OCA.
ReferenceReference
Probing protein-protein interactions. The ribose-binding protein in bacterial transport and chemotaxis., Bjorkman AJ, Binnie RA, Zhang H, Cole LB, Hermodson MA, Mowbray SL, J Biol Chem. 1994 Dec 2;269(48):30206-11. PMID:7982928
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