5ldf: Difference between revisions

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-'''Unreleased structure'''
-The entry 5ldf is ON HOLD
+==Maltose binding protein genetically fused to dodecameric glutamine synthetase==
+<StructureSection load='5ldf' size='340' side='right' caption='[[5ldf]], [[Resolution|resolution]] 6.20&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5ldf]] is a 24 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LDF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LDF FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MAL:MALTOSE'>MAL</scene></td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamate--ammonia_ligase Glutamate--ammonia ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.1.2 6.3.1.2] </span></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=5ldf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ldf OCA], [http://pdbe.org/5ldf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ldf RCSB], [http://www.ebi.ac.uk/pdbsum/5ldf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ldf ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/MALE_ECO57 MALE_ECO57]] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides (By similarity).
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Recent technical advances have revolutionized the field of cryo-electron microscopy (cryo-EM). However, most monomeric proteins remain too small (&lt;100 kDa) for cryo-EM analysis. To overcome this limitation, we explored a strategy whereby a monomeric target protein is genetically fused to a homo-oligomeric scaffold protein and the junction optimized to allow the target to adopt the scaffold symmetry, thereby generating a chimeric particle suitable for cryo-EM. To demonstrate the concept, we fused maltose-binding protein (MBP), a 40 kDa monomer, to glutamine synthetase, a dodecamer formed by two hexameric rings. Chimeric constructs with different junction lengths were screened by biophysical analysis and negative-stain EM. The optimal construct yielded a cryo-EM reconstruction that revealed the MBP structure at sub-nanometre resolution. These findings illustrate the feasibility of using homo-oligomeric scaffolds to enable cryo-EM analysis of monomeric proteins, paving the way for applying this strategy to challenging structures resistant to crystallographic and NMR analysis.
-Authors:
+Fusion to a homo-oligomeric scaffold allows cryo-EM analysis of a small protein.,Coscia F, Estrozi LF, Hans F, Malet H, Noirclerc-Savoye M, Schoehn G, Petosa C Sci Rep. 2016 Aug 3;6:30909. doi: 10.1038/srep30909. PMID:27485862<ref>PMID:27485862</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 5ldf" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Glutamate--ammonia ligase]]
+[[Category: Coscia, F]]
+[[Category: Petosa, C]]
+[[Category: Schoehn, G]]
+[[Category: Chimera]]
+[[Category: Dodecamer]]
+[[Category: Fusion protein]]
+[[Category: Ligase]]
+[[Category: Symmetrized construct]]