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==Structure of the Argonaute protein from Methanocaldcoccus janaschii in complex with guide DNA==
==Structure of the Argonaute protein from Methanocaldcoccus janaschii in complex with guide DNA==
<StructureSection load='5g5t' size='340' side='right' caption='[[5g5t]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
<StructureSection load='5g5t' size='340' side='right'caption='[[5g5t]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5g5t]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5G5T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5G5T FirstGlance]. <br>
<table><tr><td colspan='2'>[[5g5t]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5G5T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5G5T FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.85&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5g5s|5g5s]]</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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=5g5t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5g5t OCA], [http://pdbe.org/5g5t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5g5t RCSB], [http://www.ebi.ac.uk/pdbsum/5g5t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5g5t 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=5g5t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5g5t OCA], [https://pdbe.org/5g5t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5g5t RCSB], [https://www.ebi.ac.uk/pdbsum/5g5t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5g5t ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/AGO_METJA AGO_METJA] A DNA-guided ssDNA endonuclease that may play a role in defense against invading genetic elements. Uses short ssDNA sequences as guides (gDNA) to bind complementary target strands, resulting in slicing of the target DNA (tDNA) (PubMed:24442234, PubMed:27741323, PubMed:28319081, PubMed:28319084). Endonucleolytically cleaves tDNA (the gDNA indicates where to cleave); two major and two minor products are seen which correspond to cleavage sites between nucleotides 9/10, 10/11, 13/14, and 14/15 downstream of the target residue base-paired with the 5'-end of the gDNA (PubMed:24442234, PubMed:27741323, PubMed:28319081, PubMed:28319084). Efficient guide-dependent tDNA cleavage requires a minimal length of 15 bp and is maximal at 19 bp (PubMed:28319081). Prefers gDNA with 5'-phosphorylated purines and 3'-pyrimidines; changing these bases alters the cleavage activity and patterns (PubMed:28319084). Also has guide-independent activity on tDNA called 'chopping' (PubMed:28319081). Probably a first round of guide-independent activity on an invading plasmid or virus would generate guide DNAs for subsequent, more efficient, guide-dependent degradation of invading nucleic acids (PubMed:28319081). Has no activity on substrate with a mismatch at positions 10 and 11, on ssDNA or RNA, nor on DNA:RNA hybrids (PubMed:24442234). Digests longer (750 bp) dsDNA as well as circular plasmid and naked genomic DNA, but not chromatin, in a guide DNA-independent manner (PubMed:28319081). Addition of endogenous histone A3 protects DNA from cleavage, while cleavage is insensitive to methylation (PubMed:28319081). When plasmid encoding active or mutated protein (Ala-541) is transformed into Sulfolobus acidocaldarius about 25-fold fewer transformants are found with active protein; reduced levels of plasmid are found in wild-type transformed cells. While S.acidocaldarius grows at a similar temperature to M.jannaschii (70 to 80 degrees Celsius) it has very different histone-like proteins, which presumably do not protect against MjAgo (PubMed:28319081). Binds ssDNA, dsDNA and DNA-RNA hybrids; binding is most efficient with dsDNA (PubMed:24442234).<ref>PMID:24442234</ref> <ref>PMID:27741323</ref> <ref>PMID:28319081</ref> <ref>PMID:28319084</ref> <ref>PMID:28319081</ref>
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<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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==See Also==
==See Also==
*[[Argonaute|Argonaute]]
*[[Argonaute 3D structures|Argonaute 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Grohmann, D]]
[[Category: Large Structures]]
[[Category: Keegan, R]]
[[Category: Methanocaldococcus jannaschii]]
[[Category: Oellig, C A]]
[[Category: Grohmann D]]
[[Category: Schneider, S]]
[[Category: Keegan R]]
[[Category: Willkomm, S]]
[[Category: Oellig CA]]
[[Category: Zander, A]]
[[Category: Schneider S]]
[[Category: Argonaute]]
[[Category: Willkomm S]]
[[Category: Bacterial defense]]
[[Category: Zander A]]
[[Category: Hydrolase-dna complex]]

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