1dbp

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{{STRUCTURE_1dbp| PDB=1dbp | SCENE= }}
{{STRUCTURE_1dbp| PDB=1dbp | SCENE= }}
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'''IDENTICAL MUTATIONS AT CORRESPONDING POSITIONS IN TWO HOMOLOGOUS PROTEINS WITH NON-IDENTICAL EFFECTS'''
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===IDENTICAL MUTATIONS AT CORRESPONDING POSITIONS IN TWO HOMOLOGOUS PROTEINS WITH NON-IDENTICAL EFFECTS===
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==Overview==
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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.
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The line below this paragraph, {{ABSTRACT_PUBMED_8157648}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 8157648 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8157648}}
==About this Structure==
==About this Structure==
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[[Category: Mowbray, S L.]]
[[Category: Mowbray, S L.]]
[[Category: Binding protein]]
[[Category: Binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:39:48 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 22:47:14 2008''

Revision as of 19:47, 30 June 2008

Image:1dbp.png

Template:STRUCTURE 1dbp

IDENTICAL MUTATIONS AT CORRESPONDING POSITIONS IN TWO HOMOLOGOUS PROTEINS WITH NON-IDENTICAL EFFECTS

Template:ABSTRACT PUBMED 8157648

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

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