4tl1: Difference between revisions
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==GCN4-p1 with mutation to 1-Aminocyclohexanecarboxylic acid at residue 10== | ==GCN4-p1 with mutation to 1-Aminocyclohexanecarboxylic acid at residue 10== | ||
<StructureSection load='4tl1' size='340' side='right' caption='[[4tl1]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='4tl1' size='340' side='right'caption='[[4tl1]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4tl1]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TL1 OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[4tl1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TL1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TL1 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=02K:1-AMINOCYCLOHEXANECARBOXYLIC+ACID'>02K</scene>, <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4tl1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tl1 OCA], [https://pdbe.org/4tl1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4tl1 RCSB], [https://www.ebi.ac.uk/pdbsum/4tl1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4tl1 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/GCN4_YEAST GCN4_YEAST] Is a transcription factor that is responsible for the activation of more than 30 genes required for amino acid or for purine biosynthesis in response to amino acid or purine starvation. Binds and recognize the DNA sequence: 5'-TGA[CG]TCA-3'. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
*[[Gcn4|Gcn4]] | *[[Gcn4 3D Structures|Gcn4 3D Structures]] | ||
*[[Gnc4 3D Structures|Gnc4 3D Structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Saccharomyces cerevisiae S288C]] | ||
[[Category: | [[Category: Horne WS]] | ||
[[Category: | [[Category: Saxena S]] | ||
[[Category: | [[Category: Silva KI]] | ||
[[Category: | [[Category: Tavenor NA]] | ||
Latest revision as of 10:19, 27 September 2023
GCN4-p1 with mutation to 1-Aminocyclohexanecarboxylic acid at residue 10GCN4-p1 with mutation to 1-Aminocyclohexanecarboxylic acid at residue 10
Structural highlights
FunctionGCN4_YEAST Is a transcription factor that is responsible for the activation of more than 30 genes required for amino acid or for purine biosynthesis in response to amino acid or purine starvation. Binds and recognize the DNA sequence: 5'-TGA[CG]TCA-3'. Publication Abstract from PubMedModular assembly of bio-inspired supramolecular polymers is a powerful technique to develop new soft nanomaterials, and protein folding is a versatile basis for preparing such materials. Previous work demonstrated a significant difference in the physical properties of closely related supramolecular polymers composed of building blocks in which identical coiled-coil forming peptides are cross-linked by one of two subtly different organic linkers (one flexible and the other rigid). Herein, we investigate the molecular basis for this observation by isolating a single subunit of the supramolecular polymer chain and probing its structure and conformational flexibility by double electron-electron resonance (DEER) spectroscopy. Experimental spin-spin distance distributions for two different labeling sites coupled with molecular dynamics simulations provide insights into how linker structure impacts chain dynamics in the coiled-coil supramolecular polymer. Origins of Structural Flexibility in Protein-Based Supramolecular Polymers Revealed by DEER Spectroscopy.,Tavenor NA, Silva KI, Saxena S, Horne WS J Phys Chem B. 2014 Jul 24. PMID:25060334[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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