5h79: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Unreleased structure'''
-The entry 5h79 is ON HOLD  until Paper Publication
+==Crystal structure of a repeat protein with three Protein A repeat module==
+<StructureSection load='5h79' size='340' side='right'caption='[[5h79]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5h79]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H79 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5H79 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]] 2.7&#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=5h79 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h79 OCA], [https://pdbe.org/5h79 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5h79 RCSB], [https://www.ebi.ac.uk/pdbsum/5h79 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5h79 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/SPA_STAAU SPA_STAAU]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Generating artificial protein assemblies with complex shapes requires a method for connecting protein components with stable and predictable structures. Currently available methods for creating rigid protein assemblies rely on either complicated calculations or extensive trial and error. We describe a simple and efficient method for connecting two proteins via a fused alpha helix that is formed by joining two preexisting helices into a single extended helix. Because the end-to-end ligation of helices does not guarantee the formation of a continuous helix, we superimposed 1-2 turns of pairs of connecting helices by using a molecular graphics program. Then, we chose amino acids from the two natural sequences that would stabilize the connecting helix. This "shared helix method" is highly efficient. All the designed proteins that could be produced in Escherichia coli were readily crystallized and had the expected fusion structures. To prove the usefulness of this method, we produced two novel repeat proteins by assembling several copies of natural or artificial proteins with alpha helices at both termini. Their crystal structures demonstrated the successful assembly of the repeating units with the intended curved shapes. We propose that this method could dramatically expand the available repertoire of natural repeat proteins.
-Authors:
+Construction of novel repeat proteins with rigid and predictable structures using a shared helix method.,Youn SJ, Kwon NY, Lee JH, Kim JH, Choi J, Lee H, Lee JO Sci Rep. 2017 Jun 1;7(1):2595. doi: 10.1038/s41598-017-02803-z. PMID:28572639<ref>PMID:28572639</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 5h79" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Staphylococcus aureus]]
+[[Category: Kim JH]]
+[[Category: Kwon NY]]
+[[Category: Lee H]]
+[[Category: Lee JH]]
+[[Category: Lee JO]]
+[[Category: Youn SJ]]