1mow

From Proteopedia

(Difference between revisions)

Revision as of 09:53, 26 May 2021

E-DreI

Structural highlights

1mow is a 12 chain structure with sequence from desulfurococcus_mobilis Atcc 35582 desulfurococcus mobilis . Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[DMO1_DESMO] Endonuclease involved in intron homing. Recognizes a recognizes up to 20 bp of DNA in the 23S rRNA gene intron. It has a slow turnover rate and cuts the coding strand with a slight preference over the non-coding strand.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

We have generated an artificial highly specific endonuclease by fusing domains of homing endonucleases I-DmoI and I-CreI and creating a new 1400 A(2) protein interface between these domains. Protein engineering was accomplished by combining computational redesign and an in vivo protein-folding screen. The resulting enzyme, E-DreI (Engineered I-DmoI/I-CreI), binds a long chimeric DNA target site with nanomolar affinity, cleaving it precisely at a rate equivalent to its natural parents. The structure of an E-DreI/DNA complex demonstrates the accuracy of the protein interface redesign algorithm and reveals how catalytic function is maintained during the creation of the new endonuclease. These results indicate that it may be possible to generate novel highly specific DNA binding proteins from homing endonucleases.

Design, activity, and structure of a highly specific artificial endonuclease.,Chevalier BS, Kortemme T, Chadsey MS, Baker D, Monnat RJ, Stoddard BL Mol Cell. 2002 Oct;10(4):895-905. PMID:12419232^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Chevalier BS, Kortemme T, Chadsey MS, Baker D, Monnat RJ, Stoddard BL. Design, activity, and structure of a highly specific artificial endonuclease. Mol Cell. 2002 Oct;10(4):895-905. PMID:12419232

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1mow"

@@ Line 3: / Line 3: @@
 <StructureSection load='1mow' size='340' side='right'caption='[[1mow]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1mow]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_35582_[[desulfurococcus_mobilis]] Atcc 35582 [[desulfurococcus mobilis]]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MOW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MOW FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1mow]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_35582_[[desulfurococcus_mobilis]] Atcc 35582 [[desulfurococcus mobilis]]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MOW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MOW FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=1mow FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mow OCA], [http://pdbe.org/1mow PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mow RCSB], [http://www.ebi.ac.uk/pdbsum/1mow PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1mow ProSAT]</span></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=1mow FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mow OCA], [https://pdbe.org/1mow PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mow RCSB], [https://www.ebi.ac.uk/pdbsum/1mow PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mow ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/DMO1_DESMO DMO1_DESMO]] Endonuclease involved in intron homing. Recognizes a recognizes up to 20 bp of DNA in the 23S rRNA gene intron. It has a slow turnover rate and cuts the coding strand with a slight preference over the non-coding strand.
+[[https://www.uniprot.org/uniprot/DMO1_DESMO DMO1_DESMO]] Endonuclease involved in intron homing. Recognizes a recognizes up to 20 bp of DNA in the 23S rRNA gene intron. It has a slow turnover rate and cuts the coding strand with a slight preference over the non-coding strand.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1mow

From Proteopedia

Revision as of 09:53, 26 May 2021

E-DreI

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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