8wnf: Difference between revisions
New page: '''Unreleased structure''' The entry 8wnf is ON HOLD Authors: Guo, Y., Li, S., Zhang, T. Description: Crystal structures of H. pylori isoleucyl-tRNA synthetase (HpIleRS) in apo form [[... |
No edit summary |
||
| (3 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
The | ==Crystal structure of H. pylori isoleucyl-tRNA synthetase (HpIleRS) in apo form== | ||
<StructureSection load='8wnf' size='340' side='right'caption='[[8wnf]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8wnf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8WNF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8WNF FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=8wnf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8wnf OCA], [https://pdbe.org/8wnf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8wnf RCSB], [https://www.ebi.ac.uk/pdbsum/8wnf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8wnf ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/SYI_HELPY SYI_HELPY] Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile). | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Helicobacter pylori infection is a global health concern, affecting over half of the world's population. Acquiring structural information on pharmacological targets is crucial to facilitate inhibitor design. Here, we have determined the crystal structures of H. pylori isoleucyl-tRNA synthetase (HpIleRS) in apo form as well as in complex with various substrates (Ile, Ile-AMP, Val, and Val-AMP) or an inhibitor (mupirocin). Our results provide valuable insights into substrate specificity, recognition, and the mechanism by which HpIleRS is inhibited by an antibiotic. Moreover, we identified Asp641 as a prospective regulatory site and conducted biochemical analyses to investigate its regulatory mechanism. The detailed structural information acquired from this research holds promise for the development of highly selective and effective inhibitors against H. pylori infection. | |||
Structural basis for substrate and antibiotic recognition by Helicobacter pylori isoleucyl-tRNA synthetase.,Chen X, Guo Y, Shi J, Wang Y, Guo X, Wu G, Li S, Zhang T FEBS Lett. 2024 Mar;598(5):521-536. doi: 10.1002/1873-3468.14805. Epub 2024 Jan , 21. PMID:38246751<ref>PMID:38246751</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 8wnf" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Helicobacter pylori]] | |||
[[Category: Large Structures]] | |||
[[Category: Guo Y]] | |||
[[Category: Li S]] | |||
[[Category: Zhang T]] | |||
Latest revision as of 15:15, 30 October 2024
Crystal structure of H. pylori isoleucyl-tRNA synthetase (HpIleRS) in apo formCrystal structure of H. pylori isoleucyl-tRNA synthetase (HpIleRS) in apo form
Structural highlights
FunctionSYI_HELPY Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile). Publication Abstract from PubMedHelicobacter pylori infection is a global health concern, affecting over half of the world's population. Acquiring structural information on pharmacological targets is crucial to facilitate inhibitor design. Here, we have determined the crystal structures of H. pylori isoleucyl-tRNA synthetase (HpIleRS) in apo form as well as in complex with various substrates (Ile, Ile-AMP, Val, and Val-AMP) or an inhibitor (mupirocin). Our results provide valuable insights into substrate specificity, recognition, and the mechanism by which HpIleRS is inhibited by an antibiotic. Moreover, we identified Asp641 as a prospective regulatory site and conducted biochemical analyses to investigate its regulatory mechanism. The detailed structural information acquired from this research holds promise for the development of highly selective and effective inhibitors against H. pylori infection. Structural basis for substrate and antibiotic recognition by Helicobacter pylori isoleucyl-tRNA synthetase.,Chen X, Guo Y, Shi J, Wang Y, Guo X, Wu G, Li S, Zhang T FEBS Lett. 2024 Mar;598(5):521-536. doi: 10.1002/1873-3468.14805. Epub 2024 Jan , 21. PMID:38246751[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||