1dbp
From Proteopedia
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'''IDENTICAL MUTATIONS AT CORRESPONDING POSITIONS IN TWO HOMOLOGOUS PROTEINS WITH NON-IDENTICAL EFFECTS''' | '''IDENTICAL MUTATIONS AT CORRESPONDING POSITIONS IN TWO HOMOLOGOUS PROTEINS WITH NON-IDENTICAL EFFECTS''' | ||
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[[Category: Bjorkman, A J.Joakim.]] | [[Category: Bjorkman, A J.Joakim.]] | ||
[[Category: Mowbray, S L.]] | [[Category: Mowbray, S L.]] | ||
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| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:39:48 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 10:39, 2 May 2008
IDENTICAL MUTATIONS AT CORRESPONDING POSITIONS IN TWO HOMOLOGOUS PROTEINS WITH NON-IDENTICAL EFFECTS
Overview
The x-ray structure of a mutant (Gly72 to Asp) of the Escherichia coli ribose-binding protein with altered transport function has been solved and refined to 2.2-A resolution with a conventional R-factor (R-factor = [formula: see text]) of 16.0% and good stereochemistry. Comparison with the wild type ribose-binding protein shows that the structure is disturbed little at the actual mutation site, but quite appreciably in a neighboring loop. Changes in the surface of the protein at the site of mutation, however, seem to explain the functional effects. A corresponding mutation of the related glucose/galactose-binding protein has different structural and functional effects due to the different structural context of the mutation site in that protein. These results are consistent with the concept that these proteins have slightly different ways of interacting with the membrane components in transport and chemotaxis.
About this Structure
1DBP is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Identical mutations at corresponding positions in two homologous proteins with nonidentical effects., Bjorkman AJ, Binnie RA, Cole LB, Zhang H, Hermodson MA, Mowbray SL, J Biol Chem. 1994 Apr 15;269(15):11196-200. PMID:8157648 Page seeded by OCA on Fri May 2 13:39:48 2008
