1mwi

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|PDB= 1mwi |SIZE=350|CAPTION= <scene name='initialview01'>1mwi</scene>, resolution 2.35&Aring;
|PDB= 1mwi |SIZE=350|CAPTION= <scene name='initialview01'>1mwi</scene>, resolution 2.35&Aring;
|SITE=
|SITE=
-
|LIGAND=
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|LIGAND= <scene name='pdbligand=AAB:2-DEOXY-5-PHOSPHORIBOSE+GROUP'>AAB</scene>, <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>
|ACTIVITY=
|ACTIVITY=
|GENE= MUG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
|GENE= MUG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
 +
|DOMAIN=
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|RELATEDENTRY=[[1mug|1MUG]]
 +
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mwi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mwi OCA], [http://www.ebi.ac.uk/pdbsum/1mwi PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mwi RCSB]</span>
}}
}}
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[[Category: nucleotide flipping]]
[[Category: nucleotide flipping]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:49:04 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:22:14 2008''

Revision as of 19:22, 30 March 2008

Image:1mwi.gif


PDB ID 1mwi

Drag the structure with the mouse to rotate
, resolution 2.35Å
Ligands: , , , ,
Gene: MUG (Escherichia coli)
Related: 1MUG


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal structure of a MUG-DNA product complex


Overview

G:U mismatches resulting from deamination of cytosine are the most common promutagenic lesions occurring in DNA. Uracil is removed in a base-excision repair pathway by uracil DNA-glycosylase (UDG), which excises uracil from both single- and double-stranded DNA. Recently, a biochemically distinct family of DNA repair enzymes has been identified, which excises both uracil and thymine, but only from mispairs with guanine. Crystal structures of the mismatch-specific uracil DNA-glycosylase (MUG) from E. coli, and of a DNA complex, reveal a remarkable structural and functional homology to UDGs despite low sequence identity. Details of the MUG structure explain its thymine DNA-glycosylase activity and the specificity for G:U/T mispairs, which derives from direct recognition of guanine on the complementary strand.

About this Structure

1MWI is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Crystal structure of a G:T/U mismatch-specific DNA glycosylase: mismatch recognition by complementary-strand interactions., Barrett TE, Savva R, Panayotou G, Barlow T, Brown T, Jiricny J, Pearl LH, Cell. 1998 Jan 9;92(1):117-29. PMID:9489705

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