3ssw

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<StructureSection load='3ssw' size='340' side='right'caption='[[3ssw]], [[Resolution|resolution]] 1.67&Aring;' scene=''>
<StructureSection load='3ssw' size='340' side='right'caption='[[3ssw]], [[Resolution|resolution]] 1.67&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3ssw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1p6z 1p6z]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SSW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SSW FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3ssw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1p6z 1p6z]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SSW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SSW FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3ssx|3ssx]]</div></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6693&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b4393, JW4356, rtrY, trpR ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ssw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ssw OCA], [https://pdbe.org/3ssw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ssw RCSB], [https://www.ebi.ac.uk/pdbsum/3ssw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ssw ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ssw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ssw OCA], [https://pdbe.org/3ssw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ssw RCSB], [https://www.ebi.ac.uk/pdbsum/3ssw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ssw ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/TRPR_ECOLI TRPR_ECOLI]] This protein is an aporepressor. When complexed with L-tryptophan it binds the operator region of the trp operon (5'-ACTAGT-'3') and prevents the initiation of transcription. The complex also regulates trp repressor biosynthesis by binding to its regulatory region.
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[https://www.uniprot.org/uniprot/TRPR_ECOLI TRPR_ECOLI] This protein is an aporepressor. When complexed with L-tryptophan it binds the operator region of the trp operon (5'-ACTAGT-'3') and prevents the initiation of transcription. The complex also regulates trp repressor biosynthesis by binding to its regulatory region.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Extensive environment-dependent rearrangement of the helix-turn-helix DNA recognition region and adjacent L-tryptophan binding pocket is reported in the crystal structure of dimeric E. coli trp aporepressor with point mutation Leu75Phe. In one of two subunits, the eight residues immediately C-terminal to the mutation are shifted forward in helical register by three positions, and the five following residues form an extrahelical loop accommodating the register shift. In contrast, the second subunit has wildtype-like conformation, as do both subunits in an isomorphous wildtype control structure. Treated together as an ensemble pair, the distorted and wildtype-like conformations agree more fully than either conformation alone with previously reported NOE measurements on the mutant apoprotein, and account more completely for its diverse biochemical and biophysical properties. The register-shifted segment Ile79-Ala80-Thr81-Ile82-Thr83 is helical in both conformations despite low helical propensity, suggesting an important structural role for the steric constraints imposed by beta-branched residues in helical conformation.
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Environment-dependent long-range structural distortion in a temperature-sensitive point mutant.,Carey J, Benoff B, Harish B, Yuan L, Lawson CL Protein Sci. 2011 Nov 4. doi: 10.1002/pro.759. PMID:22057811<ref>PMID:22057811</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3ssw" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Ecoli]]
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[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Benoff, B]]
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[[Category: Benoff B]]
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[[Category: Berman, H M]]
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[[Category: Berman HM]]
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[[Category: Carey, J]]
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[[Category: Carey J]]
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[[Category: Lawson, C L]]
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[[Category: Lawson CL]]
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[[Category: Dna binding]]
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[[Category: Dna binding protein]]
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[[Category: Helix-turn-helix motif]]
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[[Category: Trp operator]]
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Current revision

E. coli trp aporepressor

PDB ID 3ssw

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