3a2s: Difference between revisions
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<StructureSection load='3a2s' size='340' side='right'caption='[[3a2s]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='3a2s' size='340' side='right'caption='[[3a2s]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3a2s]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3a2s]] 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=3A2S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3A2S FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FRU:FRUCTOSE'>FRU</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene>, <scene name='pdbligand=PRD_900003:sucrose'>PRD_900003</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=3a2s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a2s OCA], [https://pdbe.org/3a2s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3a2s RCSB], [https://www.ebi.ac.uk/pdbsum/3a2s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3a2s ProSAT]</span></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=3a2s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a2s OCA], [https://pdbe.org/3a2s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3a2s RCSB], [https://www.ebi.ac.uk/pdbsum/3a2s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3a2s ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q5RT80_NEIME Q5RT80_NEIME] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Neisseria meningitidis]] | |||
[[Category: Iverson TM]] | |||
[[Category: Tanabe M]] | |||
[[Category: Neisseria | |||
[[Category: | |||
[[Category: | |||
Latest revision as of 17:09, 1 November 2023
Crystal Structure of outer membrane protein PorB from Neisseria meningitidis in complex with sucroseCrystal Structure of outer membrane protein PorB from Neisseria meningitidis in complex with sucrose
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedPorB 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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