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PDBsum entry 2vld
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* Residue conservation analysis
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PDB id:
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Hydrolase
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Title:
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Crystal structure of a repair endonuclease from pyrococcus abyssi
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Structure:
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Endonuclease nucs. Chain: a, b. Synonym: nuclease for ssdna, upf0286 protein pyrab01260. Engineered: yes. Mutation: yes
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Source:
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Pyrococcus abyssi. Organism_taxid: 29292. Gene: nucs, pyrab01260, pab2263. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Expression_system_variant: codonplus-ril. Expression_system_cell_line: codonplus-ril
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Resolution:
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2.60Å
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R-factor:
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0.243
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R-free:
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0.248
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Authors:
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B.Ren,J.Kuhn,L.Meslet-Cladiere,J.Briffotaux,C.Norais,R.Lavigne, D.Flament,R.Ladenstein,H.Myllykallio
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Key ref:
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B.Ren
et al.
(2009).
Structure and function of a novel endonuclease acting on branched DNA substrates.
Embo J,
28,
2479-2489.
PubMed id:
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Date:
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14-Jan-08
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Release date:
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19-May-09
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PROCHECK
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Headers
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References
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Q9V2E8
(NUCS_PYRAB) -
Endonuclease NucS from Pyrococcus abyssi (strain GE5 / Orsay)
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Seq:
Struc:
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251 a.a.
228 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 2 residue positions (black
crosses)
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Embo J
28:2479-2489
(2009)
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PubMed id:
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Structure and function of a novel endonuclease acting on branched DNA substrates.
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B.Ren,
J.Kühn,
L.Meslet-Cladiere,
J.Briffotaux,
C.Norais,
R.Lavigne,
D.Flament,
R.Ladenstein,
H.Myllykallio.
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ABSTRACT
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We show that Pyrococcus abyssi PAB2263 (dubbed NucS (nuclease for ss DNA) is a
novel archaeal endonuclease that interacts with the replication clamp PCNA.
Structural determination of P. abyssi NucS revealed a two-domain dumbbell-like
structure that in overall does not resemble any known protein structure.
Biochemical and structural studies indicate that NucS orthologues use a
non-catalytic ssDNA-binding domain to regulate the cleavage activity at another
site, thus resulting into the specific cleavage at double-stranded DNA
(dsDNA)/ssDNA junctions on branched DNA substrates. Both 3' and 5' extremities
of the ssDNA can be cleaved at the nuclease channel that is too narrow to
accommodate duplex DNA. Altogether, our data suggest that NucS proteins
constitute a new family of structure-specific DNA endonucleases that are widely
distributed in archaea and in bacteria, including Mycobacterium tuberculosis.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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C.Creze,
R.Lestini,
J.Kühn,
A.Ligabue,
H.F.Becker,
M.Czjzek,
D.Flament,
and
H.Myllykallio
(2011).
Structure and function of a novel endonuclease acting on branched DNA substrates.
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Biochem Soc Trans,
39,
145-149.
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M.Pan,
L.M.Kelman,
and
Z.Kelman
(2011).
The archaeal PCNA proteins.
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Biochem Soc Trans,
39,
20-24.
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S.A.MacNeill
(2011).
Protein-protein interactions in the archaeal core replisome.
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Biochem Soc Trans,
39,
163-168.
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A.Groisillier,
C.Hervé,
A.Jeudy,
E.Rebuffet,
P.F.Pluchon,
Y.Chevolot,
D.Flament,
C.Geslin,
I.M.Morgado,
D.Power,
M.Branno,
H.Moreau,
G.Michel,
C.Boyen,
and
M.Czjzek
(2010).
MARINE-EXPRESS: taking advantage of high throughput cloning and expression strategies for the post-genomic analysis of marine organisms.
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Microb Cell Fact,
9,
45.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
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Links
