5app

From Proteopedia

(Difference between revisions)

Current revision

Actinobacillus actinomycetemcomitans OMP100 residues 133-198 fused to GCN4 adaptors

Structural highlights

5app is a 3 chain structure with sequence from Aggregatibacter actinomycetemcomitans D11S-1 and Saccharomyces cerevisiae S288C. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.3Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5app"

@@ Line 1: / Line 1: @@
 ==Actinobacillus actinomycetemcomitans OMP100 residues 133-198 fused to GCN4 adaptors==
-<StructureSection load='5app' size='340' side='right' caption='[[5app]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+<StructureSection load='5app' size='340' side='right'caption='[[5app]], [[Resolution|resolution]] 2.30&Aring;' 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>
+<table><tr><td colspan='2'>[[5app]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Aggregatibacter_actinomycetemcomitans_D11S-1 Aggregatibacter actinomycetemcomitans D11S-1] and [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=5APP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></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>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5app FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5app OCA], [https://pdbe.org/5app PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5app RCSB], [https://www.ebi.ac.uk/pdbsum/5app PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5app ProSAT]</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'.
+[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;">
 == Publication Abstract from PubMed ==
@@ Line 18: / Line 19: @@
 </div>
 <div class="pdbe-citations 5app" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Gcn4 3D Structures|Gcn4 3D Structures]]
+*[[Gnc4 3D Structures|Gnc4 3D Structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Alvarez, B Hernandez]]
+[[Category: Aggregatibacter actinomycetemcomitans D11S-1]]
-[[Category: Hartmann, M D]]
+[[Category: Large Structures]]
-[[Category: Lupas, A N]]
+[[Category: Saccharomyces cerevisiae S288C]]
-[[Category: Ridderbusch, O]]
+[[Category: Hartmann MD]]
-[[Category: Alpha/beta coiled coil]]
+[[Category: Hernandez Alvarez B]]
-[[Category: Beta layer]]
+[[Category: Lupas AN]]
-[[Category: Chimera]]
+[[Category: Ridderbusch O]]
-[[Category: Fusion protein]]
-[[Category: Membrane protein]]
-[[Category: Trimer]]

5app

From Proteopedia

Current revision

Actinobacillus actinomycetemcomitans OMP100 residues 133-198 fused to GCN4 adaptors

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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