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Journal article

The structures of the SNM1A and SNM1B/Apollo nuclease domains reveal a potential basis for their distinct DNA processing activities

Abstract:

The human SNM1A and SNM1B/Apollo proteins are members of an extended family of eukaryotic nuclease containing a motif related to the prokaryotic metallo-β-lactamase (MBL) fold. SNM1A is a key exonuclease during replication-dependent and transcription-coupled interstrand crosslink repair, while SNM1B/Apollo is required for maintaining telomeric overhangs. Here, we report the crystal structures of SNM1A and SNM1B at 2.16 Å. While both proteins contain a typical MBL-β-CASP domain, a region of po...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1093/nar/gkv1256

Authors


More by this author
Institution:
University of Oxford
Division:
MSD
Department:
RDM
Sub department:
Weatherall Insti. of Molecular Medicine
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
Structural Genomics Consortium
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Sub department:
Organic Chemistry
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
Structural Genomics Consortium
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Sub department:
Organic Chemistry
Role:
Author
Publisher:
Oxford University Press
Journal:
Nucleic Acids Research More from this journal
Volume:
43
Issue:
22
Pages:
11047-11060
Publication date:
2015-01-01
Acceptance date:
2015-10-30
DOI:
EISSN:
1362-4962
ISSN:
0305-1048
Pubs id:
pubs:571970
UUID:
uuid:1bb934c3-46d8-4cdd-9127-717dfc6a9740
Local pid:
pubs:571970
Source identifiers:
571970
Deposit date:
2015-12-03

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