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| | <StructureSection load='6n0s' size='340' side='right'caption='[[6n0s]], [[Resolution|resolution]] 1.92Å' scene=''> | | <StructureSection load='6n0s' size='340' side='right'caption='[[6n0s]], [[Resolution|resolution]] 1.92Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6n0s]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Stamf Stamf]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6N0S OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6N0S FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6n0s]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylothermus_marinus_F1 Staphylothermus marinus F1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6N0S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6N0S FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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]] 1.92Å</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=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Smar_0573 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=399550 STAMF])</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=6n0s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6n0s OCA], [https://pdbe.org/6n0s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6n0s RCSB], [https://www.ebi.ac.uk/pdbsum/6n0s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6n0s ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6n0s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6n0s OCA], [http://pdbe.org/6n0s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6n0s RCSB], [http://www.ebi.ac.uk/pdbsum/6n0s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6n0s ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Stamf]] | + | [[Category: Staphylothermus marinus F1]] |
| - | [[Category: Chappie, J S]] | + | [[Category: Chappie JS]] |
| - | [[Category: Hosford, C J]] | + | [[Category: Hosford CJ]] |
| - | [[Category: Niu, Y]] | + | [[Category: Niu Y]] |
| - | [[Category: Dna binding protein]]
| + | |
| - | [[Category: Eve domain]]
| + | |
| - | [[Category: Restriction endonuclease]]
| + | |
| Structural highlights
Publication Abstract from PubMed
McrBC is a conserved modification-dependent restriction system that in Escherichia coli specifically targets foreign DNA containing methylated cytosines. Crystallographic data show that the N-terminal domain of Escherichia coli McrB binds substrates via a base flipping mechanism. This region is poorly conserved among the plethora of McrB homologs, suggesting that other species may use alternative binding strategies and/or recognize different targets. Here we present the crystal structure of the N-terminal domain from Stayphlothermus marinus McrB (Sm3-180) at 1.92 A, which adopts a PUA-like EVE fold that is closely related to the YTH and ASCH RNA binding domains. Unlike most PUA-like domains, Sm3-180 binds DNA and can associate with different modified substrates. We find the canonical 'aromatic cage' binding pocket that confers specificity for methylated bases in other EVE/YTH domains is degenerate and occluded in Sm3-180, which may contribute to its promiscuity in target recognition. Further structural comparison between different PUA-like domains identifies motifs and conformational variations that correlate with the preference for binding either DNA or RNA. Together these data have important implications for PUA-like domain specificity and suggest a broader biological versatility for the McrBC family than previously described.
The N-terminal domain of Staphylothermus marinus McrB shares structural homology with PUA-like RNA binding proteins.,Hosford CJ, Adams MC, Niu Y, Chappie JS J Struct Biol. 2020 Sep 1;211(3):107572. doi: 10.1016/j.jsb.2020.107572. Epub, 2020 Jul 8. PMID:32652237[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hosford CJ, Adams MC, Niu Y, Chappie JS. The N-terminal domain of Staphylothermus marinus McrB shares structural homology with PUA-like RNA binding proteins. J Struct Biol. 2020 Sep 1;211(3):107572. doi: 10.1016/j.jsb.2020.107572. Epub, 2020 Jul 8. PMID:32652237 doi:http://dx.doi.org/10.1016/j.jsb.2020.107572
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