|
|
| (2 intermediate revisions not shown.) |
| Line 3: |
Line 3: |
| | <StructureSection load='1d02' size='340' side='right'caption='[[1d02]], [[Resolution|resolution]] 1.70Å' scene=''> | | <StructureSection load='1d02' size='340' side='right'caption='[[1d02]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1d02]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"asterococcus"_borrel_et_al._1910 "asterococcus" borrel et al. 1910]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D02 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1D02 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1d02]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycoplasma Mycoplasma]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D02 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1D02 FirstGlance]. <br> |
| - | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Type_II_site-specific_deoxyribonuclease Type II site-specific deoxyribonuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.21.4 3.1.21.4] </span></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]] 1.7Å</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=1d02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d02 OCA], [http://pdbe.org/1d02 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1d02 RCSB], [http://www.ebi.ac.uk/pdbsum/1d02 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1d02 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=1d02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d02 OCA], [https://pdbe.org/1d02 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1d02 RCSB], [https://www.ebi.ac.uk/pdbsum/1d02 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d02 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/T2MU_MYCSP T2MU_MYCSP]] Recognizes the double-stranded sequence CAATTG and cleaves after C-1. | + | [https://www.uniprot.org/uniprot/T2MU_MYCSP T2MU_MYCSP] Recognizes the double-stranded sequence CAATTG and cleaves after C-1. |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | The MunI restriction enzyme recognizes the palindromic hexanucleotide sequence C/AATTG (the '/' indicates the cleavage site). The crystal structure of its active site mutant D83A bound to cognate DNA has been determined at 1.7 A resolution. Base-specific contacts between MunI and DNA occur exclusively in the major groove. While DNA-binding sites of most other restriction enzymes are comprised of discontinuous sequence segments, MunI combines all residues involved in the base-specific contacts within one short stretch (residues R115-R121) located at the N-terminal region of the 3(10)4 helix. The outer CG base pair of the recognition sequence is recognized solely by R115 through hydrogen bonds made by backbone and side chain atoms to both bases. The mechanism of recognition of the central AATT nucleotides by MunI is similar to that of EcoRI, which recognizes the G/AATTC sequence. The local conformation of AATT deviates from the typical B-DNA form and is remarkably similar to EcoRI-DNA. It appears to be essential for specific hydrogen bonding and recognition by MunI and EcoRI.
| + | |
| - | | + | |
| - | Crystal structure of MunI restriction endonuclease in complex with cognate DNA at 1.7 A resolution.,Deibert M, Grazulis S, Janulaitis A, Siksnys V, Huber R EMBO J. 1999 Nov 1;18(21):5805-16. PMID:10545092<ref>PMID:10545092</ref>
| + | |
| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 1d02" style="background-color:#fffaf0;"></div>
| + | |
| | | | |
| | ==See Also== | | ==See Also== |
| | *[[Endonuclease 3D structures|Endonuclease 3D structures]] | | *[[Endonuclease 3D structures|Endonuclease 3D structures]] |
| - | == References == | |
| - | <references/> | |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Asterococcus borrel et al. 1910]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Type II site-specific deoxyribonuclease]] | + | [[Category: Mycoplasma]] |
| - | [[Category: Deibert, M]] | + | [[Category: Deibert M]] |
| - | [[Category: Grazulis, S]] | + | [[Category: Grazulis S]] |
| - | [[Category: Huber, R]] | + | [[Category: Huber R]] |
| - | [[Category: Janulaitis, A]] | + | [[Category: Janulaitis A]] |
| - | [[Category: Siksnys, V]] | + | [[Category: Siksnys V]] |
| - | [[Category: Alpha/beta protein]]
| + | |
| - | [[Category: Distorted double helix]]
| + | |
| - | [[Category: Hydrolase-dna complex]]
| + | |
| - | [[Category: Protein-dna complex]]
| + | |
