2asr
From Proteopedia
(New page: 200px<br /><applet load="2asr" size="450" color="white" frame="true" align="right" spinBox="true" caption="2asr, resolution 2.3Å" /> '''THE THREE-DIMENSIONAL...) |
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| - | [[Image:2asr.jpg|left|200px]]<br /><applet load="2asr" size=" | + | [[Image:2asr.jpg|left|200px]]<br /><applet load="2asr" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2asr, resolution 2.3Å" /> | caption="2asr, resolution 2.3Å" /> | ||
'''THE THREE-DIMENSIONAL STRUCTURE OF THE ASPARTATE RECEPTOR FROM ESCHERICHIA COLI'''<br /> | '''THE THREE-DIMENSIONAL STRUCTURE OF THE ASPARTATE RECEPTOR FROM ESCHERICHIA COLI'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of the periplasmic domain of the aspartate receptor | + | 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== | ==About this Structure== | ||
| - | 2ASR 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 SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 2ASR 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=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ASR OCA]. |
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Bowie, J | + | [[Category: Bowie, J U.]] |
| - | [[Category: Pakula, A | + | [[Category: Pakula, A A.]] |
| - | [[Category: Simon, M | + | [[Category: Simon, M I.]] |
[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: chemotaxis]] | [[Category: chemotaxis]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:30:47 2008'' |
Revision as of 14:30, 21 February 2008
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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 with as ligand. 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
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