View source for 3mlg


==2ouf-2x, a designed knotted protein==
<StructureSection load='3mlg' size='340' side='right'caption='[[3mlg]], [[Resolution|resolution]] 2.29&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3mlg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori_26695 Helicobacter pylori 26695]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MLG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MLG 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]] 2.29&#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=3mlg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mlg OCA], [https://pdbe.org/3mlg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mlg RCSB], [https://www.ebi.ac.uk/pdbsum/3mlg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mlg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/O25025_HELPY O25025_HELPY] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
A very small number of natural proteins have folded configurations in which the polypeptide backbone is knotted. Relatively little is known about the folding energy landscapes of such proteins, or how they have evolved. We explore those questions here by designing a unique knotted protein structure. Biophysical characterization and X-ray crystal structure determination show that the designed protein folds to the intended configuration, tying itself in a knot in the process, and that it folds reversibly. The protein folds to its native, knotted configuration approximately 20 times more slowly than a control protein, which was designed to have a similar tertiary structure but to be unknotted. Preliminary kinetic experiments suggest a complicated folding mechanism, providing opportunities for further characterization. The findings illustrate a situation where a protein is able to successfully traverse a complex folding energy landscape, though the amino acid sequence of the protein has not been subjected to evolutionary pressure for that ability. The success of the design strategy-connecting two monomers of an intertwined homodimer into a single protein chain-supports a model for evolution of knotted structures via gene duplication.

Structure and folding of a designed knotted protein.,King NP, Jacobitz AW, Sawaya MR, Goldschmidt L, Yeates TO Proc Natl Acad Sci U S A. 2010 Nov 30;107(48):20732-7. Epub 2010 Nov 10. PMID:21068371<ref>PMID:21068371</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3mlg" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Helicobacter pylori 26695]]
[[Category: Large Structures]]
[[Category: Jacobitz AW]]
[[Category: King NP]]
[[Category: Sawaya MR]]
[[Category: Yeates TO]]