5l0p: Difference between revisions

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== Function ==

[[http://www.uniprot.org/uniprot/ETV6_HUMAN ETV6_HUMAN]] Transcriptional repressor; binds to the DNA sequence 5'-CCGGAAGT-3'.

== Publication Abstract from PubMed ==

The design of proteins that self-assemble into higher order architectures is of great interest due to their potential application in nanotechnology. Specifically, the self-assembly of proteins into ordered lattices is of special interest to the field of structural biology. Here we designed a 2 dimensional (2D) protein lattice using a fusion of a tandem repeat of three TelSAM domains (TTT) to the Ferric uptake regulator (FUR) domain. We determined the structure of the designed (TTT-FUR) fusion protein to 2.3 A by X-ray crystallographic methods. In agreement with the design, a 2D lattice composed of TelSAM fibers interdigitated by the FUR domain was observed. As expected, the fusion of a tandem repeat of three TelSAM domains formed 21 screw axis, and the self-assembly of the ordered oligomer was under pH control. We demonstrated that the fusion of TTT to a domain having a 2-fold symmetry, such as the FUR domain, can produce an ordered 2D lattice. The TTT-FUR system combines features from the rotational symmetry matching approach with the oligomer driven crystallization method. This TTT-FUR fusion was amenable to X-ray crystallographic methods, and is a promising crystallization chaperone.

Symmetry based assembly of a 2 dimensional protein lattice.,Poulos S, Agah S, Jallah N, Faham S PLoS One. 2017 Apr 18;12(4):e0174485. doi: 10.1371/journal.pone.0174485., eCollection 2017. PMID:28419162<ref>PMID:28419162</ref>

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

</div>

== References ==

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 == Function ==
 [[http://www.uniprot.org/uniprot/ETV6_HUMAN ETV6_HUMAN]] Transcriptional repressor; binds to the DNA sequence 5'-CCGGAAGT-3'.
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The design of proteins that self-assemble into higher order architectures is of great interest due to their potential application in nanotechnology. Specifically, the self-assembly of proteins into ordered lattices is of special interest to the field of structural biology. Here we designed a 2 dimensional (2D) protein lattice using a fusion of a tandem repeat of three TelSAM domains (TTT) to the Ferric uptake regulator (FUR) domain. We determined the structure of the designed (TTT-FUR) fusion protein to 2.3 A by X-ray crystallographic methods. In agreement with the design, a 2D lattice composed of TelSAM fibers interdigitated by the FUR domain was observed. As expected, the fusion of a tandem repeat of three TelSAM domains formed 21 screw axis, and the self-assembly of the ordered oligomer was under pH control. We demonstrated that the fusion of TTT to a domain having a 2-fold symmetry, such as the FUR domain, can produce an ordered 2D lattice. The TTT-FUR system combines features from the rotational symmetry matching approach with the oligomer driven crystallization method. This TTT-FUR fusion was amenable to X-ray crystallographic methods, and is a promising crystallization chaperone.
+Symmetry based assembly of a 2 dimensional protein lattice.,Poulos S, Agah S, Jallah N, Faham S PLoS One. 2017 Apr 18;12(4):e0174485. doi: 10.1371/journal.pone.0174485., eCollection 2017. PMID:28419162<ref>PMID:28419162</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 5l0p" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>