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1dbp

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Revision as of 15:16, 24 December 2014

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

Structural highlights

1dbp is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[RBSB_ECOLI] Involved in the high-affinity D-ribose membrane transport system and also serves as the primary chemoreceptor for chemotaxis.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Bjorkman AJ, Binnie RA, Cole LB, Zhang H, Hermodson MA, Mowbray SL. Identical mutations at corresponding positions in two homologous proteins with nonidentical effects. J Biol Chem. 1994 Apr 15;269(15):11196-200. PMID:8157648

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1dbp"

Categories: Escherichia coli | Bjorkman, A J.Joakim | Mowbray, S L | Binding protein

@@ Line 6: / Line 6: @@
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dbp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dbp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dbp RCSB], [http://www.ebi.ac.uk/pdbsum/1dbp PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/RBSB_ECOLI RBSB_ECOLI]] Involved in the high-affinity D-ribose membrane transport system and also serves as the primary chemoreceptor for chemotaxis.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1dbp

From Proteopedia

Revision as of 15:16, 24 December 2014

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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