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PDBsum entry 2fea
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References listed in PDB file
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Key reference
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Title
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Crystal structure of mtnx phosphatase from bacillus subtilis at 2.0 angstroms resolution provides a structural basis for bipartite phosphomonoester hydrolysis of 2-Hydroxy-3-Keto-5-Methylthiopentenyl-1-Phosphate.
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Authors
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Q.Xu,
K.S.Saikatendu,
S.S.Krishna,
D.Mcmullan,
P.Abdubek,
S.Agarwalla,
E.Ambing,
T.Astakhova,
H.L.Axelrod,
D.Carlton,
H.J.Chiu,
T.Clayton,
M.Didonato,
L.Duan,
M.A.Elsliger,
J.Feuerhelm,
S.K.Grzechnik,
J.Hale,
E.Hampton,
G.W.Han,
J.Haugen,
L.Jaroszewski,
K.K.Jin,
H.E.Klock,
M.W.Knuth,
E.Koesema,
M.D.Miller,
A.T.Morse,
E.Nigoghossian,
L.Okach,
S.Oommachen,
J.Paulsen,
R.Reyes,
C.L.Rife,
R.Schwarzenbacher,
H.Van den bedem,
A.White,
G.Wolf,
K.O.Hodgson,
J.Wooley,
A.M.Deacon,
A.Godzik,
S.A.Lesley,
I.A.Wilson.
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Ref.
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Proteins, 2007,
69,
433-439.
[DOI no: ]
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PubMed id
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Abstract
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No abstract given.
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Figure 1.
Figure 1. Crystal structure of bsmtnX: (A) A simplified
schematic of the methionine salvage pathway in B. subtilis
according to the schema proposed by Sekowska et al.[2] (B)
Stereo ribbon diagram of the bsmtnX monomer color-coded from
N-terminus (blue) to C-terminus (red). Helices (H1-H12) and  -strands
1-
7)
are labeled. (C) Diagram showing the secondary structural
elements in bsmtnX superimposed on its primary sequence. The
helices, -strands,
 -turns,
and -turns
are indicated. The -hairpin
is depicted as a red loop. (D) Grasp figure showing distribution
of surface electrostatic potential (red-negative (-6kT),
blue-positive (+6kT), and white-neutral, where k is the
Boltzmann constant and T is the temperature) for bsmtnX
positioned in an orientation similar to that in (B). The bound
Mg^2+ ion is shown as a green sphere and the position of the
buried Zn^2+ ion is indicated by a shaded sphere.
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Figure 2.
Figure 2. (A) Structural superposition of bsmtnX (green), mjPSP
(PDB: 1l7p; yellow), and paThrH (PDB: 1rku; grey). The active
site aspartate, the bound phosphoserine in mjPSP, and the metal
ions are shown in ball-and-stick representation. The
zinc-binding sub-domain unique to bsmtnX is colored red and an
arrow indicates its position. The loop connecting helices H2 and
H3, which modulates transition between open/closed states, is
also colored red. (B) Structural superposition of the active
site residues of the three enzymes. Carbon atoms are colored as
in (A), oxygens are red, nitrogens are blue, and phosphate is
orange.
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The above figures are
reprinted
by permission from John Wiley & Sons, Inc.:
Proteins
(2007,
69,
433-439)
copyright 2007.
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