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1kc6

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==HincII Bound to Cognate DNA==
==HincII Bound to Cognate DNA==
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<StructureSection load='1kc6' size='340' side='right' caption='[[1kc6]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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<StructureSection load='1kc6' size='340' side='right'caption='[[1kc6]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1kc6]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacterium_influenzae"_lehmann_and_neumann_1896 "bacterium influenzae" lehmann and neumann 1896]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KC6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KC6 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1kc6]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KC6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KC6 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
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<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>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
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<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=1kc6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kc6 OCA], [http://pdbe.org/1kc6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kc6 RCSB], [http://www.ebi.ac.uk/pdbsum/1kc6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1kc6 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1kc6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kc6 OCA], [https://pdbe.org/1kc6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kc6 RCSB], [https://www.ebi.ac.uk/pdbsum/1kc6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kc6 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/T2C2_HAEIF T2C2_HAEIF]] Recognizes the double-stranded sequence GTYRAC and cleaves after Y-3.
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[https://www.uniprot.org/uniprot/T2C2_HAEIF T2C2_HAEIF] Recognizes the double-stranded sequence GTYRAC and cleaves after Y-3.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The crystal structure of the HincII restriction endonuclease-DNA complex shows that degenerate specificity for blunt-ended cleavage at GTPyPuAC sequences arises from indirect readout of conformational preferences at the center pyrimidine-purine step. Protein-induced distortion of the DNA is accomplished by intercalation of glutamine side chains into the major groove on either side of the recognition site, generating bending by either tilt or roll at three distinct loci. The intercalated side chains propagate a concerted shift of all six target-site base pairs toward the minor groove, producing an unusual cross-strand purine stacking at the center pyrimidine-purine step. Comparison of the HincII and EcoRV cocrystal structures suggests that sequence-dependent differences in base-stacking free energies are a crucial underlying factor mediating protein recognition by indirect readout.
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Sequence selectivity and degeneracy of a restriction endonuclease mediated by DNA intercalation.,Horton NC, Dorner LF, Perona JJ Nat Struct Biol. 2002 Jan;9(1):42-7. PMID:11742344<ref>PMID:11742344</ref>
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==See Also==
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*[[Endonuclease 3D structures|Endonuclease 3D structures]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1kc6" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bacterium influenzae lehmann and neumann 1896]]
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[[Category: Haemophilus influenzae]]
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[[Category: Type II site-specific deoxyribonuclease]]
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[[Category: Large Structures]]
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[[Category: Dorner, L F]]
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[[Category: Dorner LF]]
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[[Category: Horton, N C]]
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[[Category: Horton NC]]
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[[Category: Perona, J J]]
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[[Category: Perona JJ]]
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[[Category: Blunt cutting]]
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[[Category: Dna bending]]
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[[Category: Hydrolase-dna complex]]
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[[Category: Indirect readout]]
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[[Category: Protein-dna]]
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[[Category: Restriction endonuclease]]
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Current revision

HincII Bound to Cognate DNA

PDB ID 1kc6

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