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1l2c

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{{STRUCTURE_1l2c| PDB=1l2c | SCENE= }}
{{STRUCTURE_1l2c| PDB=1l2c | SCENE= }}
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'''MutM (Fpg)-DNA Estranged Thymine Mismatch Recognition Complex'''
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===MutM (Fpg)-DNA Estranged Thymine Mismatch Recognition Complex===
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==Overview==
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MutM is a bacterial 8-oxoguanine glycosylase responsible for initiating base-excision repair of oxidized guanine residues in DNA. Here we report five different crystal structures of MutM-DNA complexes that represent different steps of the repair reaction cascade catalyzed by the protein and also differ in the identity of the base opposite the lesion (the 'estranged' base). These structures reveal that the MutM active site performs the multiple steps of base-excision and 3' and 5' nicking with minimal rearrangement of the DNA backbone.
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(as it appears on PubMed at http://www.pubmed.gov), where 12055620 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12055620}}
==About this Structure==
==About this Structure==
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[[Category: Dna repair]]
[[Category: Dna repair]]
[[Category: Zinc finger]]
[[Category: Zinc finger]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:27:37 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 11:32:23 2008''

Revision as of 08:32, 2 July 2008

Image:1l2c.png

Template:STRUCTURE 1l2c

MutM (Fpg)-DNA Estranged Thymine Mismatch Recognition Complex

Template:ABSTRACT PUBMED 12055620

About this Structure

Full crystallographic information is available from OCA.

Reference

Structural insights into lesion recognition and repair by the bacterial 8-oxoguanine DNA glycosylase MutM., Fromme JC, Verdine GL, Nat Struct Biol. 2002 Jul;9(7):544-52. PMID:12055620

Page seeded by OCA on Wed Jul 2 11:32:23 2008

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