1d02: Difference between revisions
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<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=1d02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d02 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1d02 RCSB], [http://www.ebi.ac.uk/pdbsum/1d02 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=1d02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d02 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1d02 RCSB], [http://www.ebi.ac.uk/pdbsum/1d02 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/T2MU_MYCSP T2MU_MYCSP]] Recognizes the double-stranded sequence CAATTG and cleaves after C-1. | |||
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== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 19:23, 25 December 2014
CRYSTAL STRUCTURE OF MUNI RESTRICTION ENDONUCLEASE IN COMPLEX WITH COGNATE DNACRYSTAL STRUCTURE OF MUNI RESTRICTION ENDONUCLEASE IN COMPLEX WITH COGNATE DNA
Structural highlights
Function[T2MU_MYCSP] Recognizes the double-stranded sequence CAATTG and cleaves after C-1. Publication Abstract from PubMedThe MunI restriction enzyme recognizes the palindromic hexanucleotide sequence C/AATTG (the '/' indicates the cleavage site). The crystal structure of its active site mutant D83A bound to cognate DNA has been determined at 1.7 A resolution. Base-specific contacts between MunI and DNA occur exclusively in the major groove. While DNA-binding sites of most other restriction enzymes are comprised of discontinuous sequence segments, MunI combines all residues involved in the base-specific contacts within one short stretch (residues R115-R121) located at the N-terminal region of the 3(10)4 helix. The outer CG base pair of the recognition sequence is recognized solely by R115 through hydrogen bonds made by backbone and side chain atoms to both bases. The mechanism of recognition of the central AATT nucleotides by MunI is similar to that of EcoRI, which recognizes the G/AATTC sequence. The local conformation of AATT deviates from the typical B-DNA form and is remarkably similar to EcoRI-DNA. It appears to be essential for specific hydrogen bonding and recognition by MunI and EcoRI. Crystal structure of MunI restriction endonuclease in complex with cognate DNA at 1.7 A resolution.,Deibert M, Grazulis S, Janulaitis A, Siksnys V, Huber R EMBO J. 1999 Nov 1;18(21):5805-16. PMID:10545092[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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