2oz9: Difference between revisions

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[[Image:2oz9.gif|left|200px]]<br />
[[Image:2oz9.gif|left|200px]]<br /><applet load="2oz9" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="2oz9" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="2oz9, resolution 1.65&Aring;" />
caption="2oz9, resolution 1.65&Aring;" />
'''E. coli TRP holorepressor, orthorhombic crystal form'''<br />
'''E. coli TRP holorepressor, orthorhombic crystal form'''<br />


==Overview==
==Overview==
An orthorhombic crystal form of trp repressor (aporepressor plus, L-tryptophan ligand) was solved by molecular replacement, refined to 1.65, A resolution, and compared to the structure of the repressor in trigonal, crystals. Even though these two crystal forms of repressor were grown, under identical conditions, the refined structures have distinctly, different conformations of the DNA-binding domains. Unlike the, repressor/aporepressor structural transition, the conformational shift is, not caused by the binding or loss of the L-tryptophan ligand. We conclude, that while L-tryptophan binding is essential for forming a specific, complex with trp operator DNA, the corepressor ligand does not lock the, repressor into a single conformation that is complementary to the, operator. This flexibility may be required by the various binding modes, proposed for trp repressor in its search for and adherence to its three, different operator sites.
An orthorhombic crystal form of trp repressor (aporepressor plus L-tryptophan ligand) was solved by molecular replacement, refined to 1.65 A resolution, and compared to the structure of the repressor in trigonal crystals. Even though these two crystal forms of repressor were grown under identical conditions, the refined structures have distinctly different conformations of the DNA-binding domains. Unlike the repressor/aporepressor structural transition, the conformational shift is not caused by the binding or loss of the L-tryptophan ligand. We conclude that while L-tryptophan binding is essential for forming a specific complex with trp operator DNA, the corepressor ligand does not lock the repressor into a single conformation that is complementary to the operator. This flexibility may be required by the various binding modes proposed for trp repressor in its search for and adherence to its three different operator sites.


==About this Structure==
==About this Structure==
2OZ9 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 NA, SO4 and TRP as [http://en.wikipedia.org/wiki/ligands ligands]. This structure superseeds the now removed PDB entry 2WRP. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2OZ9 OCA].  
2OZ9 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=NA:'>NA</scene>, <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=TRP:'>TRP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. This structure supersedes the now removed PDB entry 2WRP. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OZ9 OCA].  


==Reference==
==Reference==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Lawson, C.L.]]
[[Category: Lawson, C L.]]
[[Category: Sigler, P.B.]]
[[Category: Sigler, P B.]]
[[Category: NA]]
[[Category: NA]]
[[Category: SO4]]
[[Category: SO4]]
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[[Category: dna binding regulatory protein]]
[[Category: dna binding regulatory protein]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:24:09 2008''

Revision as of 19:24, 21 February 2008

File:2oz9.gif


2oz9, resolution 1.65Å

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E. coli TRP holorepressor, orthorhombic crystal form

OverviewOverview

An orthorhombic crystal form of trp repressor (aporepressor plus L-tryptophan ligand) was solved by molecular replacement, refined to 1.65 A resolution, and compared to the structure of the repressor in trigonal crystals. Even though these two crystal forms of repressor were grown under identical conditions, the refined structures have distinctly different conformations of the DNA-binding domains. Unlike the repressor/aporepressor structural transition, the conformational shift is not caused by the binding or loss of the L-tryptophan ligand. We conclude that while L-tryptophan binding is essential for forming a specific complex with trp operator DNA, the corepressor ligand does not lock the repressor into a single conformation that is complementary to the operator. This flexibility may be required by the various binding modes proposed for trp repressor in its search for and adherence to its three different operator sites.

About this StructureAbout this Structure

2OZ9 is a Single protein structure of sequence from Escherichia coli with , and as ligands. This structure supersedes the now removed PDB entry 2WRP. Full crystallographic information is available from OCA.

ReferenceReference

Flexibility of the DNA-binding domains of trp repressor., Lawson CL, Zhang RG, Schevitz RW, Otwinowski Z, Joachimiak A, Sigler PB, Proteins. 1988;3(1):18-31. PMID:3375234

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