2e52: Difference between revisions
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hindIIIR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=71421 HAEIN])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hindIIIR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=71421 HAEIN])</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='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='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=2e52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e52 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2e52 RCSB], [http://www.ebi.ac.uk/pdbsum/2e52 PDBsum]</span></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=2e52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e52 OCA], [http://pdbe.org/2e52 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2e52 RCSB], [http://www.ebi.ac.uk/pdbsum/2e52 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
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<div class="pdbe-citations 2e52" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== |
Revision as of 07:29, 11 September 2015
Crystal structural analysis of HindIII restriction endonuclease in complex with cognate DNA at 2.0 angstrom resolutionCrystal structural analysis of HindIII restriction endonuclease in complex with cognate DNA at 2.0 angstrom resolution
Structural highlights
Function[T2D3_HAEIN] Recognizes the double-stranded sequence AAGCTT and cleaves after A-1. 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 PubMedThe three-dimensional crystal structures of HindIII bound to its cognate DNA with and without divalent cations were solved at 2.17 and 2.00 A resolution, respectively. HindIII forms a dimer. The structures showed that HindIII belongs to the EcoRI-like (alpha-class) subfamily of type II restriction endonucleases. The cognate DNA-complex structures revealed the specific DNA-recognition mechanism of HindIII by which it recognizes the palindromic sequence A/AGCTT. In the Mg(2+) ion-soaked structure the DNA was cleaved and two ions were bound at each active site, corresponding to the two-metal-ion mechanism. Structures of restriction endonuclease HindIII in complex with its cognate DNA and divalent cations.,Watanabe N, Takasaki Y, Sato C, Ando S, Tanaka I Acta Crystallogr D Biol Crystallogr. 2009 Dec;65(Pt 12):1326-33. doi:, 10.1107/S0907444909041134. Epub 2009 Nov 17. PMID:19966419[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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