1ynm: Difference between revisions
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==Crystal structure of restriction endonuclease HinP1I== | ==Crystal structure of restriction endonuclease HinP1I== | ||
<StructureSection load='1ynm' size='340' side='right' caption='[[1ynm]], [[Resolution|resolution]] 2.65Å' scene=''> | <StructureSection load='1ynm' size='340' side='right' caption='[[1ynm]], [[Resolution|resolution]] 2.65Å' scene=''> | ||
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hinP1IR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=727 "Bacterium influenzae" Lehmann and Neumann 1896])</td></tr> | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hinP1IR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=727 "Bacterium influenzae" Lehmann and Neumann 1896])</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=1ynm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ynm OCA], [http://pdbe.org/1ynm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ynm RCSB], [http://www.ebi.ac.uk/pdbsum/1ynm 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=1ynm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ynm OCA], [http://pdbe.org/1ynm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ynm RCSB], [http://www.ebi.ac.uk/pdbsum/1ynm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ynm ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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Revision as of 10:11, 25 April 2018
Crystal structure of restriction endonuclease HinP1ICrystal structure of restriction endonuclease HinP1I
Structural highlights
Publication Abstract from PubMedHinP1I, a type II restriction endonuclease, recognizes and cleaves a palindromic tetranucleotide sequence (G/CGC) in double-stranded DNA, producing 2 nt 5' overhanging ends. Here, we report the structure of HinP1I crystallized as one protein monomer in the crystallographic asymmetric unit. HinP1I displays an elongated shape, with a conserved catalytic core domain containing an active-site motif of SDX18QXK and a putative DNA-binding domain. Without significant sequence homology, HinP1I displays striking structural similarity to MspI, an endonuclease that cleaves a similar palindromic DNA sequence (C/CGG) and binds to that sequence crystallographically as a monomer. Almost all the structural elements of MspI can be matched in HinP1I, including both the DNA recognition and catalytic elements. Examining the protein-protein interactions in the crystal lattice, HinP1I could be dimerized through two helices located on the opposite side of the protein to the active site, generating a molecule with two active sites and two DNA-binding surfaces opposite one another on the outer surfaces of the dimer. A possible functional link between this unusual dimerization mode and the tetrameric restriction enzymes is discussed. Structure of HinP1I endonuclease reveals a striking similarity to the monomeric restriction enzyme MspI.,Yang Z, Horton JR, Maunus R, Wilson GG, Roberts RJ, Cheng X Nucleic Acids Res. 2005 Apr 1;33(6):1892-901. Print 2005. PMID:15805123[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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