View source for 5aps


==Sequence IENKKAD inserted between GCN4 adaptors - Structure A7==
<StructureSection load='5aps' size='340' side='right'caption='[[5aps]], [[Resolution|resolution]] 1.37&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5aps]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5APS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5APS FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.37&#8491;</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=5aps FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aps OCA], [https://pdbe.org/5aps PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5aps RCSB], [https://www.ebi.ac.uk/pdbsum/5aps PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5aps ProSAT]</span></td></tr>
</table>
== 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'.
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== Publication Abstract from PubMed ==
Coiled coils are the best-understood protein fold, as their backbone structure can uniquely be described by parametric equations. This level of understanding has allowed their manipulation in unprecedented detail. They do not seem a likely source of surprises, yet we describe here the unexpected formation of a new type of fiber by the simple insertion of two or six residues into the underlying heptad repeat of a parallel, trimeric coiled coil. These insertions strain the supercoil to the breaking point, causing the local formation of short beta-strands, which move the path of the chain by 120 degrees around the trimer axis. The result is an alpha/beta coiled coil, which retains only one backbone hydrogen bond per repeat unit from the parent coiled coil. Our results show that a substantially novel backbone structure is possible within the allowed regions of the Ramachandran space with only minor mutations to a known fold.

alpha/beta coiled coils.,Hartmann MD, Mendler CT, Bassler J, Karamichali I, Ridderbusch O, Lupas AN, Hernandez Alvarez B Elife. 2016 Jan 15;5. pii: e11861. doi: 10.7554/eLife.11861. PMID:26771248<ref>PMID:26771248</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 5aps" style="background-color:#fffaf0;"></div>

==See Also==
*[[Gcn4 3D Structures|Gcn4 3D Structures]]
*[[Gnc4 3D Structures|Gnc4 3D Structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Hartmann MD]]
[[Category: Hernandez Alvarez B]]
[[Category: Lupas AN]]
[[Category: Mendler CT]]