2asr

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2asr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2asr OCA], [http://www.ebi.ac.uk/pdbsum/2asr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2asr RCSB]</span>
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'''THE THREE-DIMENSIONAL STRUCTURE OF THE ASPARTATE RECEPTOR FROM ESCHERICHIA COLI'''
'''THE THREE-DIMENSIONAL STRUCTURE OF THE ASPARTATE RECEPTOR FROM ESCHERICHIA COLI'''
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[[Category: Pakula, A A.]]
[[Category: Pakula, A A.]]
[[Category: Simon, M I.]]
[[Category: Simon, M I.]]
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[[Category: chemotaxis]]
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[[Category: Chemotaxis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:26:06 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:56:51 2008''
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Revision as of 16:26, 3 May 2008

Image:2asr.jpg

Template:STRUCTURE 2asr

THE THREE-DIMENSIONAL STRUCTURE OF THE ASPARTATE RECEPTOR FROM ESCHERICHIA COLI


Overview

The crystal structure of the periplasmic domain of the aspartate receptor from Escherichia coli has been solved and refined to an R-factor of 0.203 at 2.3 A, resolution. The dimeric protein is largely helical, with four helices from each monomer forming a four-helix bundle. The dimer interface is constructed from four helices, two from each subunit, also packed together in a four-helix bundle arrangement. A sulfate ion occupies the aspartate-binding site. All hydrogen bonds made to aspartate are substituted by direct or water-mediated hydrogen bonds to the sulfate. Comparison of the Escherichia coli aspartate-receptor structure with that of Salmonella typhimurium [Milburn, Prive, Milligan, Scott, Yeh, Jancarik, Koshland & Kim (1991). Science, 254, 1342-1347; Scott, Milligan, Milburn, Prive, Yeh, Koshland & Kim (1993). J. Mol. Biol. 232, 555-573] reveals strong conservation in the structure of the monomer, but more divergence in the orientation of the subunits with respect to one another. Mutations that render the Escherichia coli receptor incapable of responding to maltose are either located in spatially conserved sites or in regions of the structures that have high temperature factors and are therefore likely to be quite flexible. The inability of the receptor from Salmonella typhimurium to respond to maltose may, therefore, be because of differences in amino acids located on the binding surface rather than structural differences.

About this Structure

2ASR is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

The three-dimensional structure of the aspartate receptor from Escherichia coli., Bowie JU, Pakula AA, Simon MI, Acta Crystallogr D Biol Crystallogr. 1995 Mar 1;51(Pt 2):145-54. PMID:15299315 Page seeded by OCA on Sat May 3 19:26:06 2008

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