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==Structure of Type IIL restriction-modification enzyme MmeI in complex with DNA has implications for engineering of new specificities==
==Structure of Type IIL restriction-modification enzyme MmeI in complex with DNA has implications for engineering of new specificities==
<StructureSection load='5hr4' size='340' side='right' caption='[[5hr4]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
<StructureSection load='5hr4' size='340' side='right'caption='[[5hr4]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5hr4]] is a 6 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HR4 FirstGlance]. <br>
<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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SFG:SINEFUNGIN'>SFG</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]] 2.5964&#8491;</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=5hr4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hr4 OCA], [http://pdbe.org/5hr4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hr4 RCSB], [http://www.ebi.ac.uk/pdbsum/5hr4 PDBsum]</span></td></tr>
<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'>[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>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/B2MU09_METME B2MU09_METME]
The 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<ref>PMID:27082731</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5hr4" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Aggarwal, A K]]
[[Category: Large Structures]]
[[Category: Callahan, S J]]
[[Category: Methylophilus methylotrophus]]
[[Category: Gupta, Y K]]
[[Category: Aggarwal AK]]
[[Category: Luyten, Y A]]
[[Category: Callahan SJ]]
[[Category: Morgan, R D]]
[[Category: Gupta YK]]
[[Category: Roberts, R J]]
[[Category: Luyten YA]]
[[Category: Wilson, G G]]
[[Category: Morgan RD]]
[[Category: Dna-protein complex]]
[[Category: Roberts RJ]]
[[Category: Hydrolase-dna complex]]
[[Category: Wilson GG]]
[[Category: Restriction-modification enzyme]]

Latest revision as of 15:32, 6 March 2024

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

5hr4 is a 6 chain structure with sequence from Methylophilus methylotrophus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.5964Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

B2MU09_METME

5hr4, resolution 2.60Å

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