1t9j

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[[Image:1t9j.gif|left|200px]]
[[Image:1t9j.gif|left|200px]]
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{{Structure
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|PDB= 1t9j |SIZE=350|CAPTION= <scene name='initialview01'>1t9j</scene>, resolution 2.00&Aring;
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The line below this paragraph, containing "STRUCTURE_1t9j", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=DA:2&#39;-DEOXYADENOSINE-5&#39;-MONOPHOSPHATE'>DA</scene>, <scene name='pdbligand=DC:2&#39;-DEOXYCYTIDINE-5&#39;-MONOPHOSPHATE'>DC</scene>, <scene name='pdbligand=DG:2&#39;-DEOXYGUANOSINE-5&#39;-MONOPHOSPHATE'>DG</scene>, <scene name='pdbligand=DT:THYMIDINE-5&#39;-MONOPHOSPHATE'>DT</scene>
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|GENE= CR.LSU INTRON OF CHOROPLAST 23S RRNA GENE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3055 Chlamydomonas reinhardtii])
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|DOMAIN=
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{{STRUCTURE_1t9j| PDB=1t9j | SCENE= }}
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|RELATEDENTRY=[[1g9y|1G9Y]], [[1g9z|1G9Z]], [[1t9i|1T9I]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1t9j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t9j OCA], [http://www.ebi.ac.uk/pdbsum/1t9j PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1t9j RCSB]</span>
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'''I-CreI(Q47E)/DNA complex'''
'''I-CreI(Q47E)/DNA complex'''
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[[Category: Sussman, D.]]
[[Category: Sussman, D.]]
[[Category: Turmel, M.]]
[[Category: Turmel, M.]]
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[[Category: dna]]
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[[Category: Dna]]
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[[Category: protein]]
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[[Category: Protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:42:28 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:53:16 2008''
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Revision as of 06:42, 3 May 2008

Image:1t9j.gif

Template:STRUCTURE 1t9j

I-CreI(Q47E)/DNA complex


Overview

The LAGLIDADG homing endonucleases include free-standing homodimers, pseudosymmetric monomers, and related enzyme domains embedded within inteins. DNA-bound structures of homodimeric I-CreI and monomeric I-SceI indicate that three catalytic divalent metal ions are distributed across a pair of overlapping active sites, with one shared metal participating in both strand cleavage reactions. These structures differ in the precise position and binding interactions of the metals. We have studied the metal dependence for the I-CreI homodimer using site-directed mutagenesis of active site residues and assays of binding affinity and cleavage activity. We have also reassessed the binding of a nonactivating metal ion (calcium) in the wild-type enzyme-substrate complex, and determined the DNA-bound structure of two inactive enzyme mutants. The conclusion of these studies is that the catalytic mechanism of symmetric LAGLIDADG homing endonucleases, and probably many of their monomeric cousins, involves a canonical two-metal mechanism in each of two active sites, which are chemically and structurally tethered to one another by a shared metal ion. Failure to occupy the shared metal site, as observed in the presence of calcium or when the metal-binding side chain from the LAGLIDADG motif (Asp 20) is mutated to asparagine, prevents cleavage by the enzyme.

About this Structure

1T9J is a Single protein structure of sequence from Chlamydomonas reinhardtii. Full crystallographic information is available from OCA.

Reference

Metal-dependent DNA cleavage mechanism of the I-CreI LAGLIDADG homing endonuclease., Chevalier B, Sussman D, Otis C, Noel AJ, Turmel M, Lemieux C, Stephens K, Monnat RJ Jr, Stoddard BL, Biochemistry. 2004 Nov 9;43(44):14015-26. PMID:15518550 Page seeded by OCA on Sat May 3 09:42:28 2008

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OCA

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