3e42: Difference between revisions
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<StructureSection load='3e42' size='340' side='right'caption='[[3e42]], [[Resolution|resolution]] 2.68Å' scene=''> | <StructureSection load='3e42' size='340' side='right'caption='[[3e42]], [[Resolution|resolution]] 2.68Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3e42]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3e42]] is a 4 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=3E42 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3E42 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.68Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | |||
<tr id=' | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3e42 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e42 OCA], [https://pdbe.org/3e42 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3e42 RCSB], [https://www.ebi.ac.uk/pdbsum/3e42 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3e42 ProSAT]</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=3e42 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e42 OCA], [https://pdbe.org/3e42 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3e42 RCSB], [https://www.ebi.ac.uk/pdbsum/3e42 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3e42 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/T2C2_HAEIF T2C2_HAEIF] Recognizes the double-stranded sequence GTYRAC and cleaves after Y-3. | |||
<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: Babic AC]] | |||
[[Category: Babic | [[Category: Horton NC]] | ||
[[Category: Horton | [[Category: Little EJ]] | ||
[[Category: Little | [[Category: Manohar VM]] | ||
[[Category: Manohar | |||
Revision as of 16:12, 26 July 2023
Q138F HincII bound to GTCGAC and Ca2+ (cocrystallized)Q138F HincII bound to GTCGAC and Ca2+ (cocrystallized)
Structural highlights
FunctionT2C2_HAEIF Recognizes the double-stranded sequence GTYRAC and cleaves after Y-3. Publication Abstract from PubMedFive new structures of the Q138F HincII enzyme bound to a total of three different DNA sequences and three different metal ions (Ca(2+), Mg(2+), and Mn(2+)) are presented. While previous structures were produced from soaking Ca(2+) into preformed Q138F HincII/DNA crystals, the new structures are derived from cocrystallization with Ca(2+), Mg(2+), or Mn(2+). The Mn(2)(+)-bound structure provides the first view of a product complex of Q138F HincII with cleaved DNA. Binding studies and a crystal structure show how Ca(2+) allows trapping of a Q138F HincII complex with noncognate DNA in a catalytically incompetent conformation. Many Q138F HincII/DNA structures show asymmetry, despite the binding of a symmetric substrate by a symmetric enzyme. The various complexes are fit into a model describing the different conformations of the DNA-bound enzyme and show how DNA conformational energetics determine DNA-cleavage rates by the Q138F HincII enzyme. DNA distortion and specificity in a sequence-specific endonuclease.,Babic AC, Little EJ, Manohar VM, Bitinaite J, Horton NC J Mol Biol. 2008 Oct 31;383(1):186-204. Epub 2008 Aug 22. PMID:18762194[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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