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PDBsum entry 1vkm
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Biosynthetic protein
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PDB id
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1vkm
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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 indigoidine synthase a (inda)-Like protein (tm1464) from thermotoga maritima at 1.90 a resolution reveals a new fold.
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Authors
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I.Levin,
M.D.Miller,
R.Schwarzenbacher,
D.Mcmullan,
P.Abdubek,
E.Ambing,
T.Biorac,
J.Cambell,
J.M.Canaves,
H.J.Chiu,
A.M.Deacon,
M.Didonato,
M.A.Elsliger,
A.Godzik,
C.Grittini,
S.K.Grzechnik,
J.Hale,
E.Hampton,
G.W.Han,
J.Haugen,
M.Hornsby,
L.Jaroszewski,
C.Karlak,
H.E.Klock,
E.Koesema,
A.Kreusch,
P.Kuhn,
S.A.Lesley,
A.Morse,
K.Moy,
E.Nigoghossian,
J.Ouyang,
R.Page,
K.Quijano,
R.Reyes,
A.Robb,
E.Sims,
G.Spraggon,
R.C.Stevens,
H.Van den bedem,
J.Velasquez,
J.Vincent,
X.Wang,
B.West,
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,
59,
864-868.
[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 TM1464. (A) Stereo ribbon
diagram of T. maritima TM1464 color-coded from N-terminus (blue)
to C-terminus (red), showing the domain organization. Helices
H1-H12, and  -strands
( 1-
11)
are indicated. (B) Diagram showing the secondary structure
elements in TM1464 superimposed on its primary sequence. The
 -helices,
3[10]-helices, -bulges,
and  -turns
are indicated. The -sheet
strands are indicated by a red A, and -hairpins
are depicted as red loops.
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Figure 2.
Figure 2. (A) The TM1464 trimer viewed along the 3-fold axis.
One subunit is shown in blue. The 3 UNLs bound to the putative
active sites are shown as red spheres. (B) TM1464 shown in
surface representation illustrating the narrow active site
pocket, with the bound UNL in ball-and-stick configuration. (C)
Close-up of the putative active site. TM1464 is shown in ribbon
representation with the UNL, manganese, and interacting residues
and waters in ball-and-stick configuration (see text). A
SigmaA-weighted Fo-Fc omit map contoured at 3.0  is
shown for the UNL, manganese, and coordinating waters. Putative
H-bond interactions between the UNL and the protein are shown in
yellow dotted lines.
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The above figures are
reprinted
by permission from John Wiley & Sons, Inc.:
Proteins
(2005,
59,
864-868)
copyright 2005.
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