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PDBsum entry 1vjo
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Contents |
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* Residue conservation analysis
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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 an alanine-Glyoxylate aminotransferase from anabaena sp. At 1.70 a resolution reveals a noncovalently linked plp cofactor.
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Authors
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G.W.Han,
R.Schwarzenbacher,
R.Page,
L.Jaroszewski,
P.Abdubek,
E.Ambing,
T.Biorac,
J.M.Canaves,
H.J.Chiu,
X.Dai,
A.M.Deacon,
M.Didonato,
M.A.Elsliger,
A.Godzik,
C.Grittini,
S.K.Grzechnik,
J.Hale,
E.Hampton,
J.Haugen,
M.Hornsby,
H.E.Klock,
E.Koesema,
A.Kreusch,
P.Kuhn,
S.A.Lesley,
I.Levin,
D.Mcmullan,
T.M.Mcphillips,
M.D.Miller,
A.Morse,
K.Moy,
E.Nigoghossian,
J.Ouyang,
J.Paulsen,
K.Quijano,
R.Reyes,
E.Sims,
G.Spraggon,
R.C.Stevens,
H.Van den bedem,
J.Velasquez,
J.Vincent,
F.Von delft,
X.Wang,
B.West,
A.White,
G.Wolf,
Q.Xu,
O.Zagnitko,
K.O.Hodgson,
J.Wooley,
I.A.Wilson.
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Ref.
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Proteins, 2005,
58,
971-975.
[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 AGT from Anabaena sp. (A) Stereo
ribbon diagram of Anabena sp. AGT color-coded from N-terminus
(blue) to C-terminus (red), showing the domain organization and
location of the putative active site (PLP molecule shown in
ball-and-stick representation). Helices H1-H15 and  -strands
( 1-
12),
as well as -sheets
A, B, and C are indicated. (B) Diagram showing the secondary
structure elements in Anabaena sp. AGT superimposed on its
primary sequence. The -sheet
designations are indicated by a red A, B, and C. Above each -strand,
-bulges
and  -turns
are indicated. -hairpins
are depicted as red loops. Disordered regions are depicted by a
dashed line, with the corresponding sequence in brackets.
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Figure 2.
Figure 2. (A) Ribbon diagram of the Anabaena sp. AGT dimer. The
N-terminal segment (red), N-terminal domain (green), and
C-terminal domain (blue) are indicated for chain A. (B)
Superposition of Anabaena sp. AGT (blue) and human AGT (PDB
code: 1h0c; gray). The corresponding bound PLP and LLP
(lysine-pyridoxal-5  -phosphate)
ligands are shown in ball-and-stick representation, and regions
of structural difference are labeled. (C) The PLP molecule bound
to the active site of Anabaena sp. AGT and interacting residues
are shown in ball-and-stick representation. 2Fo-Fc density for
PLP contoured at 1  is
shown in blue. (D) Superposition of the active sites with the
PLP and LLP molecules and interacting residues from Anabaena sp.
AGT (blue) and their counterparts in human AGT (gray, residues
labeled in brackets) in ball-and-stick representation.
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The above figures are
reprinted
by permission from John Wiley & Sons, Inc.:
Proteins
(2005,
58,
971-975)
copyright 2005.
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