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''' | ==Actinobacillus actinomycetemcomitans OMP100 residues 133-198 fused to GCN4 adaptors== | ||
<StructureSection load='5app' size='340' side='right' caption='[[5app]], [[Resolution|resolution]] 2.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5app]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5APP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5APP FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5apq|5apq]], [[5aps|5aps]], [[5apt|5apt]], [[5apu|5apu]], [[5apv|5apv]], [[5apw|5apw]], [[5apx|5apx]], [[5apy|5apy]], [[5apz|5apz]]</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5app FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5app OCA], [http://pdbe.org/5app PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5app RCSB], [http://www.ebi.ac.uk/pdbsum/5app PDBsum]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://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;"> | |||
== 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5app" style="background-color:#fffaf0;"></div> | |||
[[Category: | == References == | ||
[[Category: Hartmann, M | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Alvarez, B Hernandez]] | |||
[[Category: Hartmann, M D]] | |||
[[Category: Lupas, A N]] | |||
[[Category: Ridderbusch, O]] | [[Category: Ridderbusch, O]] | ||
[[Category: | [[Category: Alpha/beta coiled coil]] | ||
[[Category: | [[Category: Beta layer]] | ||
[[Category: Chimera]] | |||
[[Category: Fusion protein]] | |||
[[Category: Membrane protein]] | |||
[[Category: Trimer]] | |||
Revision as of 05:16, 28 January 2016
Actinobacillus actinomycetemcomitans OMP100 residues 133-198 fused to GCN4 adaptorsActinobacillus actinomycetemcomitans OMP100 residues 133-198 fused to GCN4 adaptors
Structural highlights
Function[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'. Publication Abstract from PubMedCoiled 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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