View source for 8xz3


==Mycobacterium smegmatis 50S ribosomal subunit with Erythromycin==
<StructureSection load='8xz3' size='340' side='right'caption='[[8xz3]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8xz3]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycolicibacterium_smegmatis_MC2_155 Mycolicibacterium smegmatis MC2 155]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8XZ3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8XZ3 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ERY:ERYTHROMYCIN+A'>ERY</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=8xz3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8xz3 OCA], [https://pdbe.org/8xz3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8xz3 RCSB], [https://www.ebi.ac.uk/pdbsum/8xz3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8xz3 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0QTP4_MYCS2 A0QTP4_MYCS2] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Mycobacterial HflX confers resistance against macrolide antibiotics. However, the exact molecular mechanism is poorly understood. To gain further insights, we determined the cryo-EM structures of M. smegmatis (Msm) HflX-50S subunit and 50S subunit-erythromycin (ERY) complexes at a global resolution of approximately 3 A. A conserved nucleotide A2286 at the gate of nascent peptide exit tunnel (NPET) adopts a swayed conformation in HflX-50S complex and interacts with a loop within the linker helical (LH) domain of MsmHflX that contains an additional 9 residues insertion. Interestingly, the swaying of this nucleotide, which is usually found in the non-swayed conformation, is induced by erythromycin binding. Furthermore, we observed that erythromycin decreases HflX's ribosome-dependent GTP hydrolysis, resulting in its enhanced binding and anti-association activity on the 50S subunit. Our findings reveal how mycobacterial HflX senses the presence of macrolides at the peptide tunnel entrance and confers antibiotic resistance in mycobacteria.

Cryo-EM structures reveal the molecular mechanism of HflX-mediated erythromycin resistance in mycobacteria.,Srinivasan K, Banerjee A, Sengupta J Structure. 2024 Jul 8:S0969-2126(24)00234-X. doi: 10.1016/j.str.2024.06.016. PMID:39029461<ref>PMID:39029461</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8xz3" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mycolicibacterium smegmatis MC2 155]]
[[Category: Banerjee A]]
[[Category: Sengupta J]]
[[Category: Srinivasan K]]