1wrp
From Proteopedia
(New page: 200px<br /><applet load="1wrp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wrp, resolution 2.2Å" /> '''FLEXIBILITY OF THE DN...) |
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| - | [[Image:1wrp.gif|left|200px]]<br /><applet load="1wrp" size=" | + | [[Image:1wrp.gif|left|200px]]<br /><applet load="1wrp" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1wrp, resolution 2.2Å" /> | caption="1wrp, resolution 2.2Å" /> | ||
'''FLEXIBILITY OF THE DNA-BINDING DOMAINS OF TRP REPRESSOR'''<br /> | '''FLEXIBILITY OF THE DNA-BINDING DOMAINS OF TRP REPRESSOR'''<br /> | ||
==Overview== | ==Overview== | ||
| - | An orthorhombic crystal form of trp repressor (aporepressor plus | + | 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== | ||
| - | 1WRP 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 TRP as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1WRP 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=TRP:'>TRP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WRP OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Joachimiak, A | + | [[Category: Joachimiak, A J.]] |
| - | [[Category: Lawson, C | + | [[Category: Lawson, C L.]] |
[[Category: Otwinowski, Z.]] | [[Category: Otwinowski, Z.]] | ||
| - | [[Category: Schewitz, R | + | [[Category: Schewitz, R W.]] |
| - | [[Category: Sigler, P | + | [[Category: Sigler, P B.]] |
[[Category: TRP]] | [[Category: TRP]] | ||
[[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 15:47:31 2008'' |
Revision as of 13:47, 21 February 2008
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FLEXIBILITY OF THE DNA-BINDING DOMAINS OF TRP REPRESSOR
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.
About this Structure
1WRP is a Single protein structure of sequence from Escherichia coli with as ligand. Full crystallographic information is available from OCA.
Reference
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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