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| | <StructureSection load='2pvi' size='340' side='right'caption='[[2pvi]], [[Resolution|resolution]] 1.76Å' scene=''> | | <StructureSection load='2pvi' size='340' side='right'caption='[[2pvi]], [[Resolution|resolution]] 1.76Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2pvi]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_29905 Atcc 29905]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PVI OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2PVI FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2pvi]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Proteus_vulgaris Proteus vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PVI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PVI FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=C38:5-IODO-2-DEOXY-CYTIDINE-5-MONOPHOSPHATE'>C38</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]] 1.76Å</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> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C38:5-IODO-2-DEOXY-CYTIDINE-5-MONOPHOSPHATE'>C38</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2pvi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pvi OCA], [http://pdbe.org/2pvi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2pvi RCSB], [http://www.ebi.ac.uk/pdbsum/2pvi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2pvi 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=2pvi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pvi OCA], [https://pdbe.org/2pvi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pvi RCSB], [https://www.ebi.ac.uk/pdbsum/2pvi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pvi ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/T2P2_PROHU T2P2_PROHU]] Recognizes the double-stranded sequence CAGCTG and cleaves after G-3. | + | [https://www.uniprot.org/uniprot/T2P2_PROHU T2P2_PROHU] Recognizes the double-stranded sequence CAGCTG and cleaves after G-3. |
| | <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: Atcc 29905]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Type II site-specific deoxyribonuclease]] | + | [[Category: Proteus vulgaris]] |
| - | [[Category: Cheng, X]] | + | [[Category: Cheng X]] |
| - | [[Category: Horton, J]] | + | [[Category: Horton J]] |
| - | [[Category: Hydrolase-dna complex]]
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| Structural highlights
Function
T2P2_PROHU Recognizes the double-stranded sequence CAGCTG and cleaves after G-3.
Publication Abstract from PubMed
In restriction-modification systems, cleavage of substrate sites in cellular DNA by the restriction endonuclease is prevented by the action of a cognate methyltransferase that acts on the same substrate sites. The PvuII restriction endonuclease (R.PvuII) has been structurally characterized in a complex with substrate DNA (Cheng et al., 1994) and as an apoenzyme (Athanasiadis et al., 1994). We report here a structure, determined to 1.9 A resolution by crystallography, of a complex between R.PvuII and iodinated DNA. The presence of an iodine at the 5-carbon of the methylatable cytosine results in the following changes in the protein: His84 moved away from the modified base; this movement was amplified in His85 and disrupts an intersubunit hydrogen bond; and the base modification disturbs the distribution of water molecules that associate with these histidine residues and the area of the scissile bond. Considering these observations, hypotheses are given as to why a similar oligonucleotide, where a methyl group resides on the 5-carbon of the methylatable cytosine, is slowly cleaved by R.PvuII (Rice et al., 1995).
How is modification of the DNA substrate recognized by the PvuII restriction endonuclease?,Horton JR, Bonventre J, Cheng X Biol Chem. 1998 Apr-May;379(4-5):451-8. PMID:9628337[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Horton JR, Bonventre J, Cheng X. How is modification of the DNA substrate recognized by the PvuII restriction endonuclease? Biol Chem. 1998 Apr-May;379(4-5):451-8. PMID:9628337
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