1dbp
From Proteopedia
(New page: 200px<br /><applet load="1dbp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dbp, resolution 2.2Å" /> '''IDENTICAL MUTATIONS A...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1dbp.jpg|left|200px]]<br /><applet load="1dbp" size=" | + | [[Image:1dbp.jpg|left|200px]]<br /><applet load="1dbp" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1dbp, resolution 2.2Å" /> | caption="1dbp, resolution 2.2Å" /> | ||
'''IDENTICAL MUTATIONS AT CORRESPONDING POSITIONS IN TWO HOMOLOGOUS PROTEINS WITH NON-IDENTICAL EFFECTS'''<br /> | '''IDENTICAL MUTATIONS AT CORRESPONDING POSITIONS IN TWO HOMOLOGOUS PROTEINS WITH NON-IDENTICAL EFFECTS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The x-ray structure of a mutant (Gly72 to Asp) of the Escherichia coli | + | 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== | ==About this Structure== | ||
| - | 1DBP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with RIP as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1DBP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=RIP:'>RIP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DBP OCA]. |
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Bjorkman, A | + | [[Category: Bjorkman, A J.Joakim.]] |
| - | [[Category: Mowbray, S | + | [[Category: Mowbray, S L.]] |
[[Category: RIP]] | [[Category: RIP]] | ||
[[Category: binding protein]] | [[Category: binding protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:15:00 2008'' |
Revision as of 10:15, 21 February 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 with as ligand. 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 Thu Feb 21 12:15:00 2008
