5zzm
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
<StructureSection load='5zzm' size='340' side='right' caption='[[5zzm]], [[Resolution|resolution]] 8.10Å' scene=''> | <StructureSection load='5zzm' size='340' side='right' 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/ ] 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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZZM FirstGlance]. <br> | + | <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://oca.weizmann.ac.il/oca-docs/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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ady|5ady]]</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'>[http://oca.weizmann.ac.il/oca-docs/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> | <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=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> | [[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> | ||
| + | <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> | ||
| + | |||
| + | 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__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Ecoli]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Dey, S]] | [[Category: Dey, S]] | ||
Revision as of 10:24, 5 September 2018
E. coli 50S subunit bound HflX protein in presence of ATP (AMP-PNP) and GTP (GMP-PNP) analogs.
| |||||||||||
Categories: Ecoli | Escherichia coli | Dey, S | Atpase | Heat stress | Ribosome | Rna helicase
