View source for 7mbz


==Outward facing conformation of the MetNI methionine ABC transporter in complex with lipo-MetQ==
<StructureSection load='7mbz' size='340' side='right'caption='[[7mbz]], [[Resolution|resolution]] 6.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7mbz]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_meningitidis_MC58 Neisseria meningitidis MC58]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7MBZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7MBZ 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]] 6.4&#8491;</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=7mbz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7mbz OCA], [https://pdbe.org/7mbz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7mbz RCSB], [https://www.ebi.ac.uk/pdbsum/7mbz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7mbz ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9JXP3_NEIMB Q9JXP3_NEIMB] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
NmMetQ is a substrate-binding protein (SBP) from Neisseria meningitidis that has been identified as a surface-exposed candidate antigen for meningococcal vaccines. However, this location for NmMetQ challenges the prevailing view that SBPs in Gram-negative bacteria are localized to the periplasmic space to promote interaction with their cognate ABC transporter embedded in the bacterial inner membrane. To elucidate the roles of NmMetQ, we characterized NmMetQ with and without its cognate ABC transporter (NmMetNI). Here, we show that NmMetQ is a lipoprotein (lipo-NmMetQ) that binds multiple methionine analogs and stimulates the ATPase activity of NmMetNI. Using single-particle electron cryo-microscopy, we determined the structures of NmMetNI in the presence and absence of lipo-NmMetQ. Based on our data, we propose that NmMetQ tethers to membranes via a lipid anchor and has dual function and localization, playing a role in NmMetNI-mediated transport at the inner membrane and moonlighting on the bacterial surface.

Characterization of the ABC methionine transporter from Neisseria meningitidis reveals that lipidated MetQ is required for interaction.,Sharaf NG, Shahgholi M, Kim E, Lai JY, VanderVelde DG, Lee AT, Rees DC Elife. 2021 Aug 19;10:e69742. doi: 10.7554/eLife.69742. PMID:34409939<ref>PMID:34409939</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7mbz" style="background-color:#fffaf0;"></div>

==See Also==
*[[ABC transporter 3D structures|ABC transporter 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Neisseria meningitidis MC58]]
[[Category: Rees DC]]
[[Category: Sharaf NG]]