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| <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=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[1ynm]] is a 1 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=1YNM OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1YNM FirstGlance]. <br> | | <table><tr><td colspan='2'>[[1ynm]] is a 1 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=1YNM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YNM FirstGlance]. <br> |
| </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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.65Å</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'>[https://proteopedia.org/fgij/fg.htm?mol=1ynm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ynm OCA], [https://pdbe.org/1ynm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ynm RCSB], [https://www.ebi.ac.uk/pdbsum/1ynm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ynm ProSAT]</span></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=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> |
| <div style="background-color:#fffaf0;">
| | == Function == |
| == Publication Abstract from PubMed == | | [https://www.uniprot.org/uniprot/Q5I6E6_HAEIF Q5I6E6_HAEIF] |
| HinP1I, 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.
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| 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<ref>PMID:15805123</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 1ynm" style="background-color:#fffaf0;"></div>
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| ==See Also== | | ==See Also== |
| *[[Endonuclease 3D structures|Endonuclease 3D structures]] | | *[[Endonuclease 3D structures|Endonuclease 3D structures]] |
| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Bacterium influenzae lehmann and neumann 1896]] | | [[Category: Haemophilus influenzae]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Type II site-specific deoxyribonuclease]]
| | [[Category: Cheng X]] |
| [[Category: Cheng, X]] | | [[Category: Horton JR]] |
| [[Category: Horton, J R]] | | [[Category: Maunus R]] |
| [[Category: Maunus, R]] | | [[Category: Roberts RJ]] |
| [[Category: Roberts, R J]] | | [[Category: Wilson GG]] |
| [[Category: Wilson, G G]] | | [[Category: Yang Z]] |
| [[Category: Yang, Z]] | |
| [[Category: Dimerizaton]]
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| [[Category: Hydrolase]]
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| [[Category: Restriction endonuclease]]
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