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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 n-terminal domain of e.Coli lon protease
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Structure:
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Atp-dependent protease la. Chain: a, b, c, d, e, f, g, h. Engineered: yes
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Source:
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Escherichia coli. Organism_taxid: 562. Gene: lon, capr, deg, lopa, muc. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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2.03Å
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R-factor:
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0.212
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R-free:
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0.268
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Authors:
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M.Li,F.Rasulova,E.E.Melnikov,T.V.Rotanova,A.Gustchina, M.R.Maurizi,A.Wlodawer
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Key ref:
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M.Li
et al.
(2005).
Crystal structure of the N-terminal domain of E. coli Lon protease.
Protein Sci,
14,
2895-2900.
PubMed id:
DOI:
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Date:
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11-Aug-05
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Release date:
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01-Nov-05
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PROCHECK
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Headers
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References
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P0A9M0
(LON_ECOLI) -
Lon protease
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Seq: Struc:
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784 a.a.
110 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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Enzyme class:
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E.C.3.4.21.53
- Endopeptidase La.
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Reaction:
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Hydrolysis of large proteins such as globin, casein and denaturated serum albumin, in presence of ATP.
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Gene Ontology (GO) functional annotation
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Biological process
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proteolysis
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1 term
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Biochemical function
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ATP-dependent peptidase activity
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1 term
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DOI no:
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Protein Sci
14:2895-2900
(2005)
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PubMed id:
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Crystal structure of the N-terminal domain of E. coli Lon protease.
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M.Li,
F.Rasulova,
E.E.Melnikov,
T.V.Rotanova,
A.Gustchina,
M.R.Maurizi,
A.Wlodawer.
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ABSTRACT
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We report here the first crystal structure of the N-terminal domain of an A-type
Lon protease. Lon proteases are ubiquitous, multidomain, ATP-dependent enzymes
with both highly specific and non-specific protein binding, unfolding, and
degrading activities. We expressed and purified a stable, monomeric 119-amino
acid N-terminal subdomain of the Escherichia coli A-type Lon protease and
code 2ANE).
The structure was solved in two crystal forms, yielding 14 independent views.
The domain exhibits a unique fold consisting primarily of three twisted
beta-sheets and a single long alpha-helix. Analysis of recent PDB depositions
identified a similar fold in BPP1347 (PDB code 1ZBO), a 203-amino acid protein
of unknown function from Bordetella parapertussis, crystallized as part of a
structural genomics effort. BPP1347 shares sequence homology with Lon N-domains
and with a family of other independently expressed proteins of unknown
functions. We postulate that, as is the case in Lon proteases, this structural
domain represents a general protein and polypeptide interaction domain.
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Selected figure(s)
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Figure 1.
Figure 1. Crystal structure of the N119 domain of E. coli
Lon and its comparison with the structure of the hypothetical
protein BPP1347. (A) Stereo view of LonN119 showing the elements
of the secondary structure colored green for strands, blue
for helices, and
brown for coils. (B) Superposition of LonN119 (green) and B.
parapertussis BPP1347 (gray).
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The above figure is
reprinted
by permission from the Protein Society:
Protein Sci
(2005,
14,
2895-2900)
copyright 2005.
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Figure was
selected
by the author.
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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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J.Thomas,
J.Fishovitz,
and
I.Lee
(2010).
Utilization of positional isotope exchange experiments to evaluate reversibility of ATP hydrolysis catalyzed by Escherichia coli Lon protease.
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Biochem Cell Biol, 88,
119-128.
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M.Li,
A.Gustchina,
F.S.Rasulova,
E.E.Melnikov,
M.R.Maurizi,
T.V.Rotanova,
Z.Dauter,
and
A.Wlodawer
(2010).
Structure of the N-terminal fragment of Escherichia coli Lon protease.
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Acta Crystallogr D Biol Crystallogr, 66,
865-873.
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PDB code:
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S.S.Cha,
Y.J.An,
C.R.Lee,
H.S.Lee,
Y.G.Kim,
S.J.Kim,
K.K.Kwon,
G.M.De Donatis,
J.H.Lee,
M.R.Maurizi,
and
S.G.Kang
(2010).
Crystal structure of Lon protease: molecular architecture of gated entry to a sequestered degradation chamber.
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EMBO J, 29,
3520-3530.
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N.L.Taylor,
and
A.H.Millar
(2009).
Long bugs to short plants--the Lon protease in protein stability and thermotolerance.
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New Phytol, 181,
505-508.
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B.Friguet,
A.L.Bulteau,
and
I.Petropoulos
(2008).
Mitochondrial protein quality control: implications in ageing.
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Biotechnol J, 3,
757-764.
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I.Lee,
and
C.K.Suzuki
(2008).
Functional mechanics of the ATP-dependent Lon protease- lessons from endogenous protein and synthetic peptide substrates.
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Biochim Biophys Acta, 1784,
727-735.
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M.Chruszcz,
A.Wlodawer,
and
W.Minor
(2008).
Determination of protein structures--a series of fortunate events.
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Biophys J, 95,
1-9.
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PDB code:
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D.Vineyard,
J.Patterson-Ward,
and
I.Lee
(2006).
Single-turnover kinetic experiments confirm the existence of high- and low-affinity ATPase sites in Escherichia coli Lon protease.
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Biochemistry, 45,
4602-4610.
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T.Arakaki,
I.Le Trong,
E.Phizicky,
E.Quartley,
G.DeTitta,
J.Luft,
A.Lauricella,
L.Anderson,
O.Kalyuzhniy,
E.Worthey,
P.J.Myler,
D.Kim,
D.Baker,
W.G.Hol,
and
E.A.Merritt
(2006).
Structure of Lmaj006129AAA, a hypothetical protein from Leishmania major.
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Acta Crystallogr Sect F Struct Biol Cryst Commun, 62,
175-179.
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PDB code:
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T.V.Rotanova,
I.Botos,
E.E.Melnikov,
F.Rasulova,
A.Gustchina,
M.R.Maurizi,
and
A.Wlodawer
(2006).
Slicing a protease: structural features of the ATP-dependent Lon proteases gleaned from investigations of isolated domains.
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Protein Sci, 15,
1815-1828.
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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.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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