5ldf: Difference between revisions
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==Maltose binding protein genetically fused to dodecameric glutamine synthetase== | ==Maltose binding protein genetically fused to dodecameric glutamine synthetase== | ||
<StructureSection load='5ldf' size='340' side='right' caption='[[5ldf]], [[Resolution|resolution]] 6.20Å' scene=''> | <StructureSection load='5ldf' size='340' side='right'caption='[[5ldf]], [[Resolution|resolution]] 6.20Å' scene=''> | ||
== Structural highlights == | == 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> | <table><tr><td colspan='2'>[[5ldf]] is a 24 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_typhi"_schroeter_1886 "bacillus typhi" schroeter 1886] and [http://en.wikipedia.org/wiki/Eco57 Eco57]. 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> | </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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">glnA, STY3874, t3614 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=90370 "Bacillus typhi" Schroeter 1886]), malE, Z5632, ECs5017 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83334 ECO57])</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='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> | <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> | ||
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</div> | </div> | ||
<div class="pdbe-citations 5ldf" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5ldf" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Glutamine synthetase 3D structures|Glutamine synthetase 3D structures]] | |||
*[[Maltose-binding protein|Maltose-binding protein]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bacillus typhi schroeter 1886]] | |||
[[Category: Eco57]] | |||
[[Category: Glutamate--ammonia ligase]] | [[Category: Glutamate--ammonia ligase]] | ||
[[Category: Large Structures]] | |||
[[Category: Coscia, F]] | [[Category: Coscia, F]] | ||
[[Category: Petosa, C]] | [[Category: Petosa, C]] | ||
Revision as of 13:51, 2 October 2019
Maltose binding protein genetically fused to dodecameric glutamine synthetaseMaltose binding protein genetically fused to dodecameric glutamine synthetase
Structural highlights
Function[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). Publication Abstract from PubMedRecent technical advances have revolutionized the field of cryo-electron microscopy (cryo-EM). However, most monomeric proteins remain too small (<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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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