5hr4: Difference between revisions
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<StructureSection load='5hr4' size='340' side='right'caption='[[5hr4]], [[Resolution|resolution]] 2.60Å' scene=''> | <StructureSection load='5hr4' size='340' side='right'caption='[[5hr4]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5hr4]] is a 6 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5hr4]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Methylophilus_methylotrophus Methylophilus methylotrophus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HR4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HR4 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]] 2.5964Å</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=SFG:SINEFUNGIN'>SFG</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=5hr4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hr4 OCA], [https://pdbe.org/5hr4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hr4 RCSB], [https://www.ebi.ac.uk/pdbsum/5hr4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hr4 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/B2MU09_METME B2MU09_METME] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Aggarwal | [[Category: Methylophilus methylotrophus]] | ||
[[Category: Callahan | [[Category: Aggarwal AK]] | ||
[[Category: Gupta | [[Category: Callahan SJ]] | ||
[[Category: Luyten | [[Category: Gupta YK]] | ||
[[Category: Morgan | [[Category: Luyten YA]] | ||
[[Category: Roberts | [[Category: Morgan RD]] | ||
[[Category: Wilson | [[Category: Roberts RJ]] | ||
[[Category: Wilson GG]] | |||
Revision as of 13:51, 16 August 2023
Structure of Type IIL restriction-modification enzyme MmeI in complex with DNA has implications for engineering of new specificitiesStructure of Type IIL restriction-modification enzyme MmeI in complex with DNA has implications for engineering of new specificities
Structural highlights
FunctionPublication Abstract from PubMedThe creation of restriction enzymes with programmable DNA-binding and -cleavage specificities has long been a goal of modern biology. The recently discovered Type IIL MmeI family of restriction-and-modification (RM) enzymes that possess a shared target recognition domain provides a framework for engineering such new specificities. However, a lack of structural information on Type IIL enzymes has limited the repertoire that can be rationally engineered. We report here a crystal structure of MmeI in complex with its DNA substrate and an S-adenosylmethionine analog (Sinefungin). The structure uncovers for the first time the interactions that underlie MmeI-DNA recognition and methylation (5'-TCCRAC-3'; R = purine) and provides a molecular basis for changing specificity at four of the six base pairs of the recognition sequence (5'-TCCRAC-3'). Surprisingly, the enzyme is resilient to specificity changes at the first position of the recognition sequence (5'-TCCRAC-3'). Collectively, the structure provides a basis for engineering further derivatives of MmeI and delineates which base pairs of the recognition sequence are more amenable to alterations than others. Structure of Type IIL Restriction-Modification Enzyme MmeI in Complex with DNA Has Implications for Engineering New Specificities.,Callahan SJ, Luyten YA, Gupta YK, Wilson GG, Roberts RJ, Morgan RD, Aggarwal AK PLoS Biol. 2016 Apr 15;14(4):e1002442. doi: 10.1371/journal.pbio.1002442., eCollection 2016 Apr. PMID:27082731[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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