1cmc
From Proteopedia
(New page: 200px<br /><applet load="1cmc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cmc, resolution 1.8Å" /> '''THREE DIMENSIONAL CRY...) |
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| - | [[Image:1cmc.gif|left|200px]]<br /><applet load="1cmc" size=" | + | [[Image:1cmc.gif|left|200px]]<br /><applet load="1cmc" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1cmc, resolution 1.8Å" /> | caption="1cmc, resolution 1.8Å" /> | ||
'''THREE DIMENSIONAL CRYSTAL STRUCTURES OF E. COLI MET REPRESSOR WITH AND WITHOUT COREPRESSOR'''<br /> | '''THREE DIMENSIONAL CRYSTAL STRUCTURES OF E. COLI MET REPRESSOR WITH AND WITHOUT COREPRESSOR'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The three-dimensional crystal structure of met repressor, in the presence | + | The three-dimensional crystal structure of met repressor, in the presence or absence of bound corepressor (S-adenosylmethionine), shows a dimer of intertwined monomers, which do not have the helix-turn-helix motif characteristic of other bacterial repressor and activator structures. We propose that the interaction of met repressor with DNA occurs through either a pair of symmetry-related alpha-helices or a pair of beta-strands, and suggest a model for binding of several dimers to met operator regions. |
==About this Structure== | ==About this Structure== | ||
| - | 1CMC 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 MG and SAM as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1CMC 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=MG:'>MG</scene> and <scene name='pdbligand=SAM:'>SAM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CMC OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Phillips, S | + | [[Category: Phillips, S E.V.]] |
| - | [[Category: Somers, W | + | [[Category: Somers, W S.]] |
[[Category: MG]] | [[Category: MG]] | ||
[[Category: SAM]] | [[Category: SAM]] | ||
[[Category: dna-binding regulatory protein]] | [[Category: dna-binding regulatory protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:07:30 2008'' |
Revision as of 10:07, 21 February 2008
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THREE DIMENSIONAL CRYSTAL STRUCTURES OF E. COLI MET REPRESSOR WITH AND WITHOUT COREPRESSOR
Overview
The three-dimensional crystal structure of met repressor, in the presence or absence of bound corepressor (S-adenosylmethionine), shows a dimer of intertwined monomers, which do not have the helix-turn-helix motif characteristic of other bacterial repressor and activator structures. We propose that the interaction of met repressor with DNA occurs through either a pair of symmetry-related alpha-helices or a pair of beta-strands, and suggest a model for binding of several dimers to met operator regions.
About this Structure
1CMC is a Single protein structure of sequence from Escherichia coli with and as ligands. Full crystallographic information is available from OCA.
Reference
Three-dimensional crystal structures of Escherichia coli met repressor with and without corepressor., Rafferty JB, Somers WS, Saint-Girons I, Phillips SE, Nature. 1989 Oct 26;341(6244):705-10. PMID:2677753
Page seeded by OCA on Thu Feb 21 12:07:30 2008
