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| | <StructureSection load='4q7o' size='340' side='right'caption='[[4q7o]], [[Resolution|resolution]] 1.45Å' scene=''> | | <StructureSection load='4q7o' size='340' side='right'caption='[[4q7o]], [[Resolution|resolution]] 1.45Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4q7o]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Neimb Neimb]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q7O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Q7O FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4q7o]] is a 2 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=4Q7O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Q7O FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.45Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NMB0503 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=122586 NEIMB])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4q7o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q7o OCA], [http://pdbe.org/4q7o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4q7o RCSB], [http://www.ebi.ac.uk/pdbsum/4q7o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4q7o 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=4q7o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q7o OCA], [https://pdbe.org/4q7o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4q7o RCSB], [https://www.ebi.ac.uk/pdbsum/4q7o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4q7o ProSAT]</span></td></tr> |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/Q7DDN8_NEIMB Q7DDN8_NEIMB] |
| - | Contact-dependent growth inhibition (CDI) is an important mechanism of intercellular competition between neighboring Gram-negative bacteria. CDI systems encode large surface-exposed CdiA effector proteins that carry a variety of C-terminal toxin domains (CdiA-CTs). All CDI(+) bacteria also produce CdiI immunity proteins that specifically bind to the cognate CdiA-CT and neutralize its toxin activity to prevent auto-inhibition. Here, the X-ray crystal structure of a CdiI immunity protein from Neisseria meningitidis MC58 is presented at 1.45 A resolution. The CdiI protein has structural homology to the Whirly family of RNA-binding proteins, but appears to lack the characteristic nucleic acid-binding motif of this family. Sequence homology suggests that the cognate CdiA-CT is related to the eukaryotic EndoU family of RNA-processing enzymes. A homology model is presented of the CdiA-CT based on the structure of the XendoU nuclease from Xenopus laevis. Molecular-docking simulations predict that the CdiA-CT toxin active site is occluded upon binding to the CdiI immunity protein. Together, these observations suggest that the immunity protein neutralizes toxin activity by preventing access to RNA substrates.
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| - | | + | |
| - | The structure of a contact-dependent growth-inhibition (CDI) immunity protein from Neisseria meningitidis MC58.,Tan K, Johnson PM, Stols L, Boubion B, Eschenfeldt W, Babnigg G, Hayes CS, Joachimiak A, Goulding CW Acta Crystallogr F Struct Biol Commun. 2015 Jun 1;71(Pt 6):702-9. doi:, 10.1107/S2053230X15006585. Epub 2015 May 20. PMID:26057799<ref>PMID:26057799</ref>
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| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 4q7o" style="background-color:#fffaf0;"></div>
| + | |
| - | == References ==
| + | |
| - | <references/>
| + | |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Neimb]] | + | [[Category: Neisseria meningitidis MC58]] |
| - | [[Category: Babnigg, G]] | + | [[Category: Babnigg G]] |
| - | [[Category: Eschenfeldt, W]] | + | [[Category: Eschenfeldt W]] |
| - | [[Category: Goulding, C W]] | + | [[Category: Goulding CW]] |
| - | [[Category: Hayes, C S]] | + | [[Category: Hayes CS]] |
| - | [[Category: Joachimiak, A]] | + | [[Category: Joachimiak A]] |
| - | [[Category: Low, D A]] | + | [[Category: Low DA]] |
| - | [[Category: Structural genomic]]
| + | [[Category: Stols L]] |
| - | [[Category: Stols, L]] | + | [[Category: Tan K]] |
| - | [[Category: Tan, K]] | + | |
| - | [[Category: UC4CDI, Structure-Function Analysis of Polymorphic CDI Toxin-Immunity Protein Complexes]]
| + | |
| - | [[Category: Immune system]]
| + | |
| - | [[Category: Mcsg]]
| + | |
| - | [[Category: PSI, Protein structure initiative]]
| + | |
| - | [[Category: Psi-biology]]
| + | |
| - | [[Category: Structure-function analysis of polymorphic cdi toxin-immunity protein complex]]
| + | |
| - | [[Category: Uc4cdi]]
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