1ynm: Difference between revisions
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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 [ | <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> | </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'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q5I6E6_HAEIF Q5I6E6_HAEIF] | |||
<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: | [[Category: Haemophilus influenzae]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Cheng X]] | |||
[[Category: Cheng | [[Category: Horton JR]] | ||
[[Category: Horton | [[Category: Maunus R]] | ||
[[Category: Maunus | [[Category: Roberts RJ]] | ||
[[Category: Roberts | [[Category: Wilson GG]] | ||
[[Category: Wilson | [[Category: Yang Z]] | ||
[[Category: Yang | |||
Revision as of 09:38, 26 October 2022
Crystal structure of restriction endonuclease HinP1ICrystal structure of restriction endonuclease HinP1I
Structural highlights
FunctionPublication 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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