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| | <SX load='5ldf' size='340' side='right' viewer='molstar' caption='[[5ldf]], [[Resolution|resolution]] 6.20Å' scene=''> | | <SX load='5ldf' size='340' side='right' viewer='molstar' caption='[[5ldf]], [[Resolution|resolution]] 6.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <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://proteopedia.org/fgij/fg.htm?mol=5LDF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5ldf]] is a 24 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7 Escherichia coli O157:H7] and [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhi Salmonella enterica subsp. enterica serovar Typhi]. 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 [https://proteopedia.org/fgij/fg.htm?mol=5LDF FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MAL:MALTOSE'>MAL</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 6.2Å</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900001:alpha-maltose'>PRD_900001</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'>[https://proteopedia.org/fgij/fg.htm?mol=5ldf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ldf OCA], [https://pdbe.org/5ldf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ldf RCSB], [https://www.ebi.ac.uk/pdbsum/5ldf PDBsum], [https://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://proteopedia.org/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> | | </table> |
| | == Function == | | == 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). | + | [https://www.uniprot.org/uniprot/GLN1B_SALTI GLN1B_SALTI] Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia.[UniProtKB:P0A1P6] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </SX> | | </SX> |
| - | [[Category: Bacillus typhi schroeter 1886]] | + | [[Category: Escherichia coli O157:H7]] |
| - | [[Category: Eco57]]
| + | |
| - | [[Category: Glutamate--ammonia ligase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Coscia, F]] | + | [[Category: Salmonella enterica subsp. enterica serovar Typhi]] |
| - | [[Category: Petosa, C]] | + | [[Category: Coscia F]] |
| - | [[Category: Schoehn, G]] | + | [[Category: Petosa C]] |
| - | [[Category: Chimera]] | + | [[Category: Schoehn G]] |
| - | [[Category: Dodecamer]]
| + | |
| - | [[Category: Fusion protein]]
| + | |
| - | [[Category: Ligase]]
| + | |
| - | [[Category: Symmetrized construct]]
| + | |
| Structural highlights
Function
GLN1B_SALTI Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia.[UniProtKB:P0A1P6]
Publication Abstract from PubMed
Recent 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 Also
References
- ↑ Coscia F, Estrozi LF, Hans F, Malet H, Noirclerc-Savoye M, Schoehn G, Petosa C. Fusion to a homo-oligomeric scaffold allows cryo-EM analysis of a small protein. Sci Rep. 2016 Aug 3;6:30909. doi: 10.1038/srep30909. PMID:27485862 doi:http://dx.doi.org/10.1038/srep30909
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