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| <StructureSection load='5b7i' size='340' side='right'caption='[[5b7i]], [[Resolution|resolution]] 2.60Å' scene=''> | | <StructureSection load='5b7i' size='340' side='right'caption='[[5b7i]], [[Resolution|resolution]] 2.60Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[5b7i]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B7I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5B7I FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5b7i]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_UCBPP-PA14 Pseudomonas aeruginosa UCBPP-PA14] and [https://en.wikipedia.org/wiki/Pseudomonas_phage_JBD5 Pseudomonas phage JBD5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B7I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5B7I FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</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]] 2.6Å</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> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <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=5b7i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b7i OCA], [http://pdbe.org/5b7i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5b7i RCSB], [http://www.ebi.ac.uk/pdbsum/5b7i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5b7i 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=5b7i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b7i OCA], [https://pdbe.org/5b7i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5b7i RCSB], [https://www.ebi.ac.uk/pdbsum/5b7i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5b7i ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[http://www.uniprot.org/uniprot/CAS3_PSEAB CAS3_PSEAB]] CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Cas3 plus Cascade participate in CRISPR interference, the third stage of CRISPR immunity (Potential). In this bacteria Y.pestis-subtype CRISPRs do not confer resistance to phage DSM3 or MP22, but instead are required for DMS3-dependent inhibition of biofilm formation and possibly motility.<ref>PMID:21398535</ref> | + | [https://www.uniprot.org/uniprot/CAS3_PSEAB CAS3_PSEAB] CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Cas3 plus Cascade participate in CRISPR interference, the third stage of CRISPR immunity (Potential). In this bacteria Y.pestis-subtype CRISPRs do not confer resistance to phage DSM3 or MP22, but instead are required for DMS3-dependent inhibition of biofilm formation and possibly motility.<ref>PMID:21398535</ref> |
| <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: Wang, X]] | + | [[Category: Pseudomonas aeruginosa UCBPP-PA14]] |
- | [[Category: Zhu, Y]]
| + | [[Category: Pseudomonas phage JBD5]] |
- | [[Category: Anti-crispr]]
| + | [[Category: Wang X]] |
- | [[Category: Dna nuclease]] | + | [[Category: Zhu Y]] |
- | [[Category: Hydrolase-unknown function complex]] | + | |
- | [[Category: Phagy protein]] | + | |
| Structural highlights
Function
CAS3_PSEAB CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Cas3 plus Cascade participate in CRISPR interference, the third stage of CRISPR immunity (Potential). In this bacteria Y.pestis-subtype CRISPRs do not confer resistance to phage DSM3 or MP22, but instead are required for DMS3-dependent inhibition of biofilm formation and possibly motility.[1]
Publication Abstract from PubMed
Bacteriophages express proteins that inactivate the CRISPR-Cas bacterial immune system. Here we report the crystal structure of the anti-CRISPR protein AcrF3 in complex with Pseudomonas aeruginosa Cas3 (PaCas3). AcrF3 forms a homodimer that locks PaCas3 in an ADP-bound form, blocks the entrance of the DNA-binding tunnel in the helicase domain, and masks the linker region and C-terminal domain of PaCas3, thereby preventing recruitment by Cascade and inhibiting the type I-F CRISPR-Cas system.
Structural basis of Cas3 inhibition by the bacteriophage protein AcrF3.,Wang X, Yao D, Xu JG, Li AR, Xu J, Fu P, Zhou Y, Zhu Y Nat Struct Mol Biol. 2016 Jul 25. doi: 10.1038/nsmb.3269. PMID:27455460[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Cady KC, O'Toole GA. Non-identity-mediated CRISPR-bacteriophage interaction mediated via the Csy and Cas3 proteins. J Bacteriol. 2011 Jul;193(14):3433-45. doi: 10.1128/JB.01411-10. Epub 2011 Mar, 11. PMID:21398535 doi:http://dx.doi.org/10.1128/JB.01411-10
- ↑ Wang X, Yao D, Xu JG, Li AR, Xu J, Fu P, Zhou Y, Zhu Y. Structural basis of Cas3 inhibition by the bacteriophage protein AcrF3. Nat Struct Mol Biol. 2016 Jul 25. doi: 10.1038/nsmb.3269. PMID:27455460 doi:http://dx.doi.org/10.1038/nsmb.3269
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