View source for 7de8


==Crystal Structure of outer membrane protein PorB with G103K mutations from Neisseria meningitidis W135==
<StructureSection load='7de8' size='340' side='right'caption='[[7de8]], [[Resolution|resolution]] 2.76&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7de8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_meningitidis Neisseria meningitidis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7DE8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DE8 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]] 2.76&#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=7de8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7de8 OCA], [https://pdbe.org/7de8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7de8 RCSB], [https://www.ebi.ac.uk/pdbsum/7de8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7de8 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/M4GGR4_NEIME M4GGR4_NEIME] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Gram-negative bacteria cause the majority of highly drug-resistant bacterial infections. To cross the outer membrane of the complex Gram-negative cell envelope, antibiotics permeate through porins, trimeric channel proteins that enable the exchange of small polar molecules. Mutations in porins contribute to the development of drug-resistant phenotypes. In this work, we show that a single point mutation in the porin PorB from Neisseria meningitidis, the causative agent of bacterial meningitis, can strongly affect the binding and permeation of beta-lactam antibiotics. Using X-ray crystallography, high-resolution electrophysiology, atomistic biomolecular simulation, and liposome swelling experiments, we demonstrate differences in drug binding affinity, ion selectivity and drug permeability of PorB. Our work further reveals distinct interactions between the transversal electric field in the porin eyelet and the zwitterionic drugs, which manifest themselves under applied electric fields in electrophysiology and are altered by the mutation. These observations may apply more broadly to drug-porin interactions in other channels. Our results improve the molecular understanding of porin-based drug-resistance in Gram-negative bacteria.

An antibiotic-resistance conferring mutation in a neisserial porin: Structure, ion flux, and ampicillin binding.,Bartsch A, Ives CM, Kattner C, Pein F, Diehn M, Tanabe M, Munk A, Zachariae U, Steinem C, Llabres S Biochim Biophys Acta Biomembr. 2021 Jun 1;1863(6):183601. doi:, 10.1016/j.bbamem.2021.183601. Epub 2021 Mar 3. PMID:33675718<ref>PMID:33675718</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7de8" style="background-color:#fffaf0;"></div>

==See Also==
*[[Porin 3D structures|Porin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Neisseria meningitidis]]
[[Category: Kattner C]]
[[Category: Tanabe M]]