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| | <StructureSection load='6n05' size='340' side='right'caption='[[6n05]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='6n05' size='340' side='right'caption='[[6n05]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6n05]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"diplokokkus_intracellularis_meningitidis"_(sic)_weichselbaum_1887 "diplokokkus intracellularis meningitidis" (sic) weichselbaum 1887]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6N05 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6N05 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6n05]] is a 2 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=6N05 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6N05 FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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]] 2.5Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">COH52_04850 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=487 "Diplokokkus intracellularis meningitidis" (sic) Weichselbaum 1887])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=6n05 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6n05 OCA], [http://pdbe.org/6n05 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6n05 RCSB], [http://www.ebi.ac.uk/pdbsum/6n05 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6n05 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=6n05 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6n05 OCA], [https://pdbe.org/6n05 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6n05 RCSB], [https://www.ebi.ac.uk/pdbsum/6n05 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6n05 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A425B3G2_NEIME A0A425B3G2_NEIME] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Maxwell, K L]] | + | [[Category: Neisseria meningitidis]] |
| - | [[Category: Moraes, T F]] | + | [[Category: Maxwell KL]] |
| - | [[Category: Shah, M]] | + | [[Category: Moraes TF]] |
| - | [[Category: Thavalingham, A]] | + | [[Category: Shah M]] |
| - | [[Category: Prophage protein. anti-crispr]] | + | [[Category: Thavalingham A]] |
| - | [[Category: Viral protein]]
| + | |
| Structural highlights
Function
A0A425B3G2_NEIME
Publication Abstract from PubMed
CRISPR-Cas adaptive immune systems function to protect bacteria from invasion by foreign genetic elements. The CRISPR-Cas9 system has been widely adopted as a powerful genome-editing tool, and phage-encoded inhibitors, known as anti-CRISPRs, offer a means of regulating its activity. Here, we report the crystal structures of anti-CRISPR protein AcrIIC2Nme alone and in complex with Nme1Cas9. We demonstrate that AcrIIC2Nme inhibits Cas9 through interactions with the positively charged bridge helix, thereby preventing sgRNA loading. In vivo phage plaque assays and in vitro DNA cleavage assays show that AcrIIC2Nme mediates its activity through a large electronegative surface. This work shows that anti-CRISPR activity can be mediated through the inhibition of Cas9 complex assembly.
Inhibition of CRISPR-Cas9 ribonucleoprotein complex assembly by anti-CRISPR AcrIIC2.,Thavalingam A, Cheng Z, Garcia B, Huang X, Shah M, Sun W, Wang M, Harrington L, Hwang S, Hidalgo-Reyes Y, Sontheimer EJ, Doudna J, Davidson AR, Moraes TF, Wang Y, Maxwell KL Nat Commun. 2019 Jun 26;10(1):2806. doi: 10.1038/s41467-019-10577-3. PMID:31243272[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Thavalingam A, Cheng Z, Garcia B, Huang X, Shah M, Sun W, Wang M, Harrington L, Hwang S, Hidalgo-Reyes Y, Sontheimer EJ, Doudna J, Davidson AR, Moraes TF, Wang Y, Maxwell KL. Inhibition of CRISPR-Cas9 ribonucleoprotein complex assembly by anti-CRISPR AcrIIC2. Nat Commun. 2019 Jun 26;10(1):2806. doi: 10.1038/s41467-019-10577-3. PMID:31243272 doi:http://dx.doi.org/10.1038/s41467-019-10577-3
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