3vzi: Difference between revisions
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<StructureSection load='3vzi' size='340' side='right'caption='[[3vzi]], [[Resolution|resolution]] 2.66Å' scene=''> | <StructureSection load='3vzi' size='340' side='right'caption='[[3vzi]], [[Resolution|resolution]] 2.66Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3vzi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3vzi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Xanthomonas_oryzae_pv._oryzae_PXO99A Xanthomonas oryzae pv. oryzae PXO99A]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VZI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VZI 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]] 2.66Å</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=3vzi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vzi OCA], [https://pdbe.org/3vzi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vzi RCSB], [https://www.ebi.ac.uk/pdbsum/3vzi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vzi 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=3vzi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vzi OCA], [https://pdbe.org/3vzi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vzi RCSB], [https://www.ebi.ac.uk/pdbsum/3vzi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vzi ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A0J9X178_XANOP A0A0J9X178_XANOP] 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 spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA).[PIRNR:PIRNR029950] | |||
<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: | [[Category: Xanthomonas oryzae pv. oryzae PXO99A]] | ||
[[Category: Bae | [[Category: Bae E]] | ||
[[Category: Koo | [[Category: Koo Y]] | ||
Latest revision as of 15:43, 8 November 2023
Crystal Structure of CRISPR-associated ProteinCrystal Structure of CRISPR-associated Protein
Structural highlights
FunctionA0A0J9X178_XANOP 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 spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA).[PIRNR:PIRNR029950] Publication Abstract from PubMedClustered regularly interspaced short palindromic repeats (CRISPRs) and CRISPR-associated (Cas) proteins form an RNA-mediated microbial immune system against invading foreign genetic elements. Cas5 proteins constitute one of the most prevalent Cas protein families in CRISPR-Cas systems and are predicted to have RNA recognition motif (RRM) domains. Cas5d is a subtype I-C-specific Cas5 protein that can be divided into two distinct subgroups, one of which has extra C-terminal residues while the other contains a longer insertion in the middle of its N-terminal RRM domain. Here, we report crystal structures of Cas5d from Streptococcus pyogenes and Xanthomonas oryzae, which respectively represent the two Cas5d subgroups. Despite a common domain architecture consisting of an N-terminal RRM domain and a C-terminal beta-sheet domain, the structural differences between the two Cas5d proteins are highlighted by the presence of a unique extended helical region protruding from the N-terminal RRM domain of X. oryzae Cas5d. We also demonstrate that Cas5d proteins possess not only specific endoribonuclease activity for CRISPR RNAs but also nonspecific double-stranded DNA binding affinity. These findings suggest that Cas5d may play multiple roles in CRISPR-mediated immunity. Furthermore, the specific RNA processing was also observed between S. pyogenes Cas5d protein and X. oryzae CRISPR RNA and vice versa. This cross-species activity of Cas5d provides a special opportunity for elucidating conserved features of the CRISPR RNA processing event. Conservation and Variability in the Structure and Function of the Cas5d Endoribonuclease in the CRISPR-Mediated Microbial Immune System.,Koo Y, Ka D, Kim EJ, Suh N, Bae E J Mol Biol. 2013 Oct 23;425(20):3799-810. doi: 10.1016/j.jmb.2013.02.032. Epub, 2013 Mar 7. PMID:23500492[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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