View source for 3vzu


==Crystal Structure of outer membrane protein PorB from Neisseria meningitidis in complex with AMP-PNP==
<StructureSection load='3vzu' size='340' side='right'caption='[[3vzu]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3vzu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_meningitidis Neisseria meningitidis]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3a2u 3a2u]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VZU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VZU 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]] 2.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</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=3vzu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vzu OCA], [https://pdbe.org/3vzu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vzu RCSB], [https://www.ebi.ac.uk/pdbsum/3vzu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vzu ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/M4GGR4_NEIME M4GGR4_NEIME] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
PorB is the second most prevalent outer membrane protein in Neisseria meningitidis. PorB is required for neisserial pathogenesis and can elicit a Toll-like receptor mediated host immune response. Here, the x-ray crystal structure of PorB has been determined to 2.3 A resolution. Structural analysis and cocrystallization studies identify three putative solute translocation pathways through the channel pore: One pathway transports anions nonselectively, one transports cations nonselectively, and one facilitates the specific uptake of sugars. During infection, PorB likely binds host mitochondrial ATP, and cocrystallization with the ATP analog AMP-PNP suggests that binding of nucleotides regulates these translocation pathways both by partial occlusion of the pore and by restricting the motion of a putative voltage gating loop. PorB is located on the surface of N. meningitidis and can be recognized by receptors of the host innate immune system. Features of PorB suggest that Toll-like receptor mediated recognition outer membrane proteins may be initiated with a nonspecific electrostatic attraction.

Structural basis for solute transport, nucleotide regulation, and immunological recognition of Neisseria meningitidis PorB.,Tanabe M, Nimigean CM, Iverson TM Proc Natl Acad Sci U S A. 2010 Apr 13;107(15):6811-6. Epub 2010 Mar 29. PMID:20351243<ref>PMID:20351243</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3vzu" style="background-color:#fffaf0;"></div>

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