5ybb: Difference between revisions
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==Structural basis underlying complex assembly andconformational transition of the type I R-M system== | |||
<StructureSection load='5ybb' size='340' side='right'caption='[[5ybb]], [[Resolution|resolution]] 3.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5ybb]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Caldanaerobacter_subterraneus_subsp._tengcongensis_MB4 Caldanaerobacter subterraneus subsp. tengcongensis MB4] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YBB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YBB FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></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=5ybb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ybb OCA], [https://pdbe.org/5ybb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ybb RCSB], [https://www.ebi.ac.uk/pdbsum/5ybb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ybb ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q8R9Q4_CALS4 Q8R9Q4_CALS4] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Type I restriction-modification (R-M) systems are multisubunit enzymes with separate DNA-recognition (S), methylation (M), and restriction (R) subunits. Despite extensive studies spanning five decades, the detailed molecular mechanisms underlying subunit assembly and conformational transition are still unclear due to the lack of high-resolution structural information. Here, we report the atomic structure of a type I MTase complex (2M+1S) bound to DNA and cofactor S-adenosyl methionine in the "open" form. The intermolecular interactions between M and S subunits are mediated by a four-helix bundle motif, which also determines the specificity of the interaction. Structural comparison between open and previously reported low-resolution "closed" structures identifies the huge conformational changes within the MTase complex. Furthermore, biochemical results show that R subunits prefer to load onto the closed form MTase. Based on our results, we proposed an updated model for the complex assembly. The work reported here provides guidelines for future applications in molecular biology. | |||
Structural basis underlying complex assembly and conformational transition of the type I R-M system.,Liu YP, Tang Q, Zhang JZ, Tian LF, Gao P, Yan XX Proc Natl Acad Sci U S A. 2017 Oct 17;114(42):11151-11156. doi:, 10.1073/pnas.1711754114. Epub 2017 Oct 2. PMID:28973912<ref>PMID:28973912</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5ybb" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Endonuclease 3D structures|Endonuclease 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Caldanaerobacter subterraneus subsp. tengcongensis MB4]] | |||
[[Category: Large Structures]] | |||
[[Category: Synthetic construct]] | |||
[[Category: Gao P]] | |||
[[Category: Liu YP]] | |||
[[Category: Tang Q]] | |||
[[Category: Tian LF]] | |||
[[Category: Yan XX]] | |||
[[Category: Zhang JZ]] | |||
Latest revision as of 15:21, 6 November 2024
Structural basis underlying complex assembly andconformational transition of the type I R-M systemStructural basis underlying complex assembly andconformational transition of the type I R-M system
Structural highlights
FunctionPublication Abstract from PubMedType I restriction-modification (R-M) systems are multisubunit enzymes with separate DNA-recognition (S), methylation (M), and restriction (R) subunits. Despite extensive studies spanning five decades, the detailed molecular mechanisms underlying subunit assembly and conformational transition are still unclear due to the lack of high-resolution structural information. Here, we report the atomic structure of a type I MTase complex (2M+1S) bound to DNA and cofactor S-adenosyl methionine in the "open" form. The intermolecular interactions between M and S subunits are mediated by a four-helix bundle motif, which also determines the specificity of the interaction. Structural comparison between open and previously reported low-resolution "closed" structures identifies the huge conformational changes within the MTase complex. Furthermore, biochemical results show that R subunits prefer to load onto the closed form MTase. Based on our results, we proposed an updated model for the complex assembly. The work reported here provides guidelines for future applications in molecular biology. Structural basis underlying complex assembly and conformational transition of the type I R-M system.,Liu YP, Tang Q, Zhang JZ, Tian LF, Gao P, Yan XX Proc Natl Acad Sci U S A. 2017 Oct 17;114(42):11151-11156. doi:, 10.1073/pnas.1711754114. Epub 2017 Oct 2. PMID:28973912[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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