5e5o: Difference between revisions
No edit summary |
No edit summary |
||
| (2 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==I-SmaMI bound to uncleaved DNA target in the presence of Calcium ions== | ==I-SmaMI bound to uncleaved DNA target in the presence of Calcium ions== | ||
<StructureSection load='5e5o' size='340' side='right' caption='[[5e5o]], [[Resolution|resolution]] 2.36Å' scene=''> | <StructureSection load='5e5o' size='340' side='right'caption='[[5e5o]], [[Resolution|resolution]] 2.36Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5e5o]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E5O OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5e5o]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Sordaria_macrospora_k-hell Sordaria macrospora k-hell] 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=5E5O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5E5O 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]] 2.36Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5e5o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e5o OCA], [https://pdbe.org/5e5o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5e5o RCSB], [https://www.ebi.ac.uk/pdbsum/5e5o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5e5o ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/F7WD42_SORMK F7WD42_SORMK] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 16: | Line 19: | ||
</div> | </div> | ||
<div class="pdbe-citations 5e5o" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5e5o" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Endonuclease 3D structures|Endonuclease 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Sordaria macrospora k-hell]] | ||
[[Category: Synthetic construct]] | |||
[[Category: | [[Category: Shen BW]] | ||
[[Category: | |||
Latest revision as of 09:13, 5 July 2023
I-SmaMI bound to uncleaved DNA target in the presence of Calcium ionsI-SmaMI bound to uncleaved DNA target in the presence of Calcium ions
Structural highlights
FunctionPublication Abstract from PubMedLAGLIDADG homing endonucleases ("meganucleases") are highly specific DNA cleaving enzymes that are used for genome engineering. Like other enzymes that act on DNA targets, meganucleases often display binding affinities and cleavage activities that are dominated by one protein domain. To decipher the underlying mechanism of asymmetric DNA recognition and catalysis, we identified and characterized a new monomeric meganuclease (I-SmaMI), which belongs to a superfamily of homologous enzymes that recognize divergent DNA sequences. We solved a series of crystal structures of the enzyme-DNA complex representing a progression of sequential reaction states, and we compared the structural rearrangements and surface potential distributions within each protein domain against their relative contribution to binding affinity. We then determined the effects of equivalent point mutations in each of the two enzyme active sites to determine whether asymmetry in DNA recognition is translated into corresponding asymmetry in DNA cleavage activity. These experiments demonstrate the structural basis for "dominance" by one protein domain over the other and provide insights into this enzyme's conformational switch from a nonspecific search mode to a more specific recognition mode. The Structural Basis of Asymmetry in DNA Binding and Cleavage as Exhibited by the I-SmaMI LAGLIDADG Meganuclease.,Shen BW, Lambert A, Walker BC, Stoddard BL, Kaiser BK J Mol Biol. 2015 Dec 15. pii: S0022-2836(15)00696-8. doi:, 10.1016/j.jmb.2015.12.005. PMID:26705195[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||