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| <StructureSection load='1myk' size='340' side='right'caption='[[1myk]], [[Resolution|resolution]] 2.40Å' scene=''> | | <StructureSection load='1myk' size='340' side='right'caption='[[1myk]], [[Resolution|resolution]] 2.40Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[1myk]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpp22 Bpp22]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MYK OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1MYK FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1myk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_virus_P22 Salmonella virus P22]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MYK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MYK FirstGlance]. <br> |
- | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MUTATED ARC GENE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10754 BPP22])</td></tr> | + | </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=1myk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1myk OCA], [https://pdbe.org/1myk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1myk RCSB], [https://www.ebi.ac.uk/pdbsum/1myk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1myk ProSAT]</span></td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1myk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1myk OCA], [http://pdbe.org/1myk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1myk RCSB], [http://www.ebi.ac.uk/pdbsum/1myk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1myk ProSAT]</span></td></tr> | + | |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[http://www.uniprot.org/uniprot/RARC_BPP22 RARC_BPP22]] This protein acts as a transcriptional repressor of its own gene arc and of gene ant. | + | [[https://www.uniprot.org/uniprot/RARC_BPP22 RARC_BPP22]] This protein acts as a transcriptional repressor of its own gene arc and of gene ant. |
- | <div style="background-color:#fffaf0;">
| + | |
- | == Publication Abstract from PubMed ==
| + | |
- | Arc repressor is a small, dimeric DNA-binding protein that belongs to the ribbon-helix-helix family of transcription factors. Replacing Pro8 at the N-terminal end of the beta-sheet with leucine increases the stability of the mutant protein by 2.5 kcal/mol of dimer. However, this enhanced stability is achieved at the expense of significantly reduced DNA binding affinity. The structure of the PL8 mutant dimer has been determined to 2.4-A resolution by X-ray crystallography. The overall structure of the mutant is very similar to wild type, but Leu8 makes an additional interstrand hydrogen bond at each end of the beta-sheet of the mutant, increasing the total number of beta-sheet hydrogen bonds from six to eight. Comparison of the refolding and unfolding kinetics of the PL8 mutant and wild-type Arc shows that the enhanced stability of the mutant is accounted for by a decrease in the rate of protein unfolding, suggesting that the mutation acts to stabilize the native state and that the beta-sheet forms after the rate-limiting step in folding. The reduced operator affinity of the PL8 dimer appears to arise because the mutant cannot make the new interstrand hydrogen bonds and simultaneously make the wild-type set of contacts with operator DNA.
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- | Crystal structure, folding, and operator binding of the hyperstable Arc repressor mutant PL8.,Schildbach JF, Milla ME, Jeffrey PD, Raumann BE, Sauer RT Biochemistry. 1995 Jan 31;34(4):1405-12. PMID:7827088<ref>PMID:7827088</ref>
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- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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- | </div>
| + | |
- | <div class="pdbe-citations 1myk" style="background-color:#fffaf0;"></div>
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| | | |
| ==See Also== | | ==See Also== |
| *[[Myosin 3D Structures|Myosin 3D Structures]] | | *[[Myosin 3D Structures|Myosin 3D Structures]] |
- | == References == | |
- | <references/> | |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Bpp22]] | |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Jeffrey, P D]] | + | [[Category: Salmonella virus P22]] |
- | [[Category: Milla, M E]] | + | [[Category: Jeffrey PD]] |
- | [[Category: Raumann, B E]] | + | [[Category: Milla ME]] |
- | [[Category: Sauer, R T]] | + | [[Category: Raumann BE]] |
- | [[Category: Schildbach, J F]] | + | [[Category: Sauer RT]] |
- | [[Category: Transcription regulation]] | + | [[Category: Schildbach JF]] |