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| | <SX load='5zzm' size='340' side='right' viewer='molstar' caption='[[5zzm]], [[Resolution|resolution]] 8.10Å' scene=''> | | <SX load='5zzm' size='340' side='right' viewer='molstar' caption='[[5zzm]], [[Resolution|resolution]] 8.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5zzm]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli] and [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZZM OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5ZZM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5zzm]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZZM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZZM FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ady|5ady]]</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]] 8.1Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hflX, b4173, JW4131 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=5zzm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zzm OCA], [https://pdbe.org/5zzm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zzm RCSB], [https://www.ebi.ac.uk/pdbsum/5zzm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zzm 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=5zzm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zzm OCA], [http://pdbe.org/5zzm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zzm RCSB], [http://www.ebi.ac.uk/pdbsum/5zzm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zzm ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/HFLX_ECOLI HFLX_ECOLI]] GTPase that associates with the 50S ribosomal subunit and may have a role during protein synthesis or ribosome biogenesis. In vitro, also exhibits ATPase activity.[HAMAP-Rule:MF_00900]<ref>PMID:19109926</ref> <ref>PMID:19181811</ref> <ref>PMID:19824612</ref> | + | [https://www.uniprot.org/uniprot/HFLX_ECOLI HFLX_ECOLI] GTPase that associates with the 50S ribosomal subunit and may have a role during protein synthesis or ribosome biogenesis. In vitro, also exhibits ATPase activity.[HAMAP-Rule:MF_00900]<ref>PMID:19109926</ref> <ref>PMID:19181811</ref> <ref>PMID:19824612</ref> |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | The ribosome-associated GTPase HflX acts as an antiassociation factor upon binding to the 50S ribosomal subunit during heat stress in Escherichia coli Although HflX is recognized as a guanosine triphosphatase, several studies have shown that the N-terminal domain 1 of HflX is capable of hydrolyzing adenosine triphosphate (ATP), but the functional role of its adenosine triphosphatase (ATPase) activity remains unknown. We demonstrate that E. coli HflX possesses ATP-dependent RNA helicase activity and is capable of unwinding large subunit ribosomal RNA. A cryo-electron microscopy structure of the 50S-HflX complex in the presence of nonhydrolyzable analogues of ATP and guanosine triphosphate hints at a mode of action for the RNA helicase and suggests the linker helical domain may have a determinant role in RNA unwinding. Heat stress results in inactivation of the ribosome, and we show that HflX can restore heat-damaged ribosomes and improve cell survival.
| + | |
| | | | |
| - | The universally conserved GTPase HflX is an RNA helicase that restores heat-damaged Escherichia coli ribosomes.,Dey S, Biswas C, Sengupta J J Cell Biol. 2018 Jul 2;217(7):2519-2529. doi: 10.1083/jcb.201711131. Epub 2018, Jun 21. PMID:29930203<ref>PMID:29930203</ref>
| + | ==See Also== |
| - | | + | *[[GTP-binding protein 3D structures|GTP-binding protein 3D structures]] |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 5zzm" style="background-color:#fffaf0;"></div>
| + | |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </SX> | | </SX> |
| - | [[Category: Ecoli]] | |
| | [[Category: Escherichia coli]] | | [[Category: Escherichia coli]] |
| | + | [[Category: Escherichia coli K-12]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Dey, S]] | + | [[Category: Dey S]] |
| - | [[Category: Atpase]]
| + | |
| - | [[Category: Heat stress]]
| + | |
| - | [[Category: Ribosome]]
| + | |
| - | [[Category: Rna helicase]]
| + | |
