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6nmd

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Current revision (09:21, 20 March 2024) (edit) (undo)
 
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<SX load='6nmd' size='340' side='right' viewer='molstar' caption='[[6nmd]], [[Resolution|resolution]] 3.49&Aring;' scene=''>
<SX load='6nmd' size='340' side='right' viewer='molstar' caption='[[6nmd]], [[Resolution|resolution]] 3.49&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6nmd]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_baa-1259 Atcc baa-1259] and [http://en.wikipedia.org/wiki/Lachnospiraceae_bacterium_nd2006 Lachnospiraceae bacterium nd2006]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NMD OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6NMD FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6nmd]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Lachnospiraceae_bacterium_ND2006 Lachnospiraceae bacterium ND2006] and [https://en.wikipedia.org/wiki/Moraxella_bovoculi Moraxella bovoculi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NMD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6NMD FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.49&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AAX09_07405 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=386891 ATCC BAA-1259])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6nmd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nmd OCA], [http://pdbe.org/6nmd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6nmd RCSB], [http://www.ebi.ac.uk/pdbsum/6nmd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6nmd ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6nmd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nmd OCA], [https://pdbe.org/6nmd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6nmd RCSB], [https://www.ebi.ac.uk/pdbsum/6nmd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6nmd ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/A0A182DWE3_9FIRM A0A182DWE3_9FIRM]
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CRISPR-Cas12a (Cpf1), a type V CRISPR-associated nuclease, provides bacterial immunity against bacteriophages and plasmids but also serves as a tool for genome editing. Foreign nucleic acids are integrated into the CRISPR locus, prompting transcription of CRISPR RNAs (crRNAs) that guide Cas12a cleavage of foreign complementary DNA. However, mobile genetic elements counteract Cas12a with inhibitors, notably type V-A anti-CRISPRs (AcrVAs). We present cryoelectron microscopy structures of Cas12a-crRNA bound to AcrVA1 and AcrVA4 at 3.5 and 3.3 A resolutions, respectively. AcrVA1 is sandwiched between the recognition (REC) and nuclease (NUC) lobes of Cas12a and inserts into the binding pocket for the protospacer-adjacent motif (PAM), a short DNA sequence guiding Cas12a targeting. AcrVA1 cleaves crRNA in a Cas12a-dependent manner, inactivating Cas12a-crRNA complexes. The AcrVA4 dimer is anchored around the crRNA pseudoknot of Cas12a-crRNA, preventing required conformational changes for crRNA-DNA heteroduplex formation. These results uncover molecular mechanisms for CRISPR-Cas12a inhibition, providing insights into bacteria-phage dynamics.
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Structural Basis for the Inhibition of CRISPR-Cas12a by Anti-CRISPR Proteins.,Zhang H, Li Z, Daczkowski CM, Gabel C, Mesecar AD, Chang L Cell Host Microbe. 2019 May 27. pii: S1931-3128(19)30249-5. doi:, 10.1016/j.chom.2019.05.004. PMID:31155345<ref>PMID:31155345</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6nmd" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</SX>
</SX>
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[[Category: Atcc baa-1259]]
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[[Category: Lachnospiraceae bacterium ND2006]]
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[[Category: Lachnospiraceae bacterium nd2006]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Chang, L]]
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[[Category: Moraxella bovoculi]]
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[[Category: Li, Z]]
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[[Category: Chang L]]
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[[Category: Zhang, H]]
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[[Category: Li Z]]
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[[Category: Unknown function-rna complex]]
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[[Category: Zhang H]]

Current revision

cryo-EM Structure of the LbCas12a-crRNA-AcrVA1 complex

6nmd, resolution 3.49Å

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