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* Residue conservation analysis
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Gene Ontology (GO) functional annotation
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Biological process
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carbohydrate metabolic process
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1 term
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Biochemical function
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catalytic activity
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2 terms
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DOI no:
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FEBS Lett
580:2646-2652
(2006)
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PubMed id:
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Crystal structure of AmyA lacks acidic surface and provide insights into protein stability at poly-extreme condition.
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N.Sivakumar,
N.Li,
J.W.Tang,
B.K.Patel,
K.Swaminathan.
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ABSTRACT
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Here we report the first crystal structure of a protein, AmyA, a secretory
alpha-amylase isolated from Halothermothrix orenii, which is both halophilic and
thermophilic. The crystal structure was determined at 1.6 A resolution. AmyA
lacks the conserved acidic surface, which is considered essential for protein
stability at high salinity. Sedimentation velocity and CD experiments on AmyA
reveal the formation of unique reversible poly-dispersed oligomers that show
unusually high thermal stability. These studies provide valuable insight into
the structural elements that contribute to the stability of AmyA at both
physical and chemical extremes and their functional implications.
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Selected figure(s)
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The above figure is
reprinted
by permission from the Federation of European Biochemical Societies:
FEBS Lett
(2006,
580,
2646-2652)
copyright 2006.
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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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F.Liu,
J.Xiong,
S.Kumar,
C.Yang,
S.Ge,
S.Li,
N.Xia,
and
K.Swaminathan
(2011).
Structural and biophysical characterization of Mycobacterium tuberculosis dodecin Rv1498A.
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J Struct Biol, 175,
31-38.
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PDB code:
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R.Yamaguchi,
H.Tokunaga,
M.Ishibashi,
T.Arakawa,
and
M.Tokunaga
(2011).
Salt-dependent thermo-reversible α-amylase: cloning and characterization of halophilic α-amylase from moderately halophilic bacterium, Kocuria varians.
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Appl Microbiol Biotechnol, 89,
673-684.
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M.Ghollasi,
K.Khajeh,
H.Naderi-Manesh,
and
A.Ghasemi
(2010).
Engineering of a Bacillus alpha-amylase with improved thermostability and calcium independency.
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Appl Biochem Biotechnol, 162,
444-459.
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N.M.Koropatkin,
and
T.J.Smith
(2010).
SusG: a unique cell-membrane-associated alpha-amylase from a prominent human gut symbiont targets complex starch molecules.
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Structure, 18,
200-215.
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PDB codes:
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J.A.Winter,
P.Christofi,
S.Morroll,
and
K.A.Bunting
(2009).
The crystal structure of Haloferax volcanii proliferating cell nuclear antigen reveals unique surface charge characteristics due to halophilic adaptation.
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BMC Struct Biol, 9,
55.
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PDB code:
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K.Mavromatis,
N.Ivanova,
I.Anderson,
A.Lykidis,
S.D.Hooper,
H.Sun,
V.Kunin,
A.Lapidus,
P.Hugenholtz,
B.Patel,
and
N.C.Kyrpides
(2009).
Genome analysis of the anaerobic thermohalophilic bacterium Halothermothrix orenii.
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PLoS ONE, 4,
e4192.
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S.Srimathi,
G.Jayaraman,
G.Feller,
B.Danielsson,
and
P.R.Narayanan
(2007).
Intrinsic halotolerance of the psychrophilic alpha-amylase from Pseudoalteromonas haloplanktis.
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Extremophiles, 11,
505-515.
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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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