 |
PDBsum entry 1o2d
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Oxidoreductase
|
PDB id
|
|
|
|
1o2d
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Crystal structure of an iron-Containing 1,3-Propanediol dehydrogenase (tm0920) from thermotoga maritima at 1.3 a resolution.
|
|
|
Authors
|
|
R.Schwarzenbacher,
F.Von delft,
J.M.Canaves,
L.S.Brinen,
X.Dai,
A.M.Deacon,
M.A.Elsliger,
S.Eshaghi,
R.Floyd,
A.Godzik,
C.Grittini,
S.K.Grzechnik,
C.Guda,
L.Jaroszewski,
C.Karlak,
H.E.Klock,
E.Koesema,
J.S.Kovarik,
A.Kreusch,
P.Kuhn,
S.A.Lesley,
D.Mcmullan,
T.M.Mcphillips,
M.A.Miller,
M.D.Miller,
A.Morse,
K.Moy,
J.Ouyang,
R.Page,
A.Robb,
K.Rodrigues,
T.L.Selby,
G.Spraggon,
R.C.Stevens,
H.Van den bedem,
J.Velasquez,
J.Vincent,
X.Wang,
B.West,
G.Wolf,
K.O.Hodgson,
J.Wooley,
I.A.Wilson.
|
|
|
Ref.
|
|
Proteins, 2004,
54,
174-177.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
No abstract given.
|
|
|
|
|
|
|
|
Figure 1.
Figure 1. Crystal structure of TM0920. A: Ribbon diagram of
Thermotoga maritima TM0920 1,3-propanediol dehydrogenase color
coded from N-terminus (blue) to C-terminus (red) showing the
domain organization and location of the active site (arrow).
 -helices
(H1-H19) and  -strands
( 1-
8)
are indicated. The NADP^+ molecule is shown in ball and stick.
The Fe^2+ ion is shown as a sphere in magenta. B: Diagram
showing the secondary structure elements in TM0920 superimposed
on its primary sequence. Residues located in the active site and
interacting with Fe^2+ are indicated by blue dots and green
triangles. Residues interacting with NADP^+ are indicated by red
dots. The location of the -hairpin
formed by -strands
6 and 7 is depicted in red.
|
|
Figure 2.
Figure 2. A: Schematic representation of the interactions
between NADP^+ and its interacting residues. The NADP^+ molecule
is depicted in purple and the protein residues are in orange.
The atoms are indicated as follows: carbon (black), oxygen
(red), nitrogen (blue), and phosphorus (purple). Hydrogen bonds
are represented as dashed green lines. Residues implicated in
hydrophobic interaction are represented as barbed circle
sections. B: Close-up view of the active site showing residues
coordinating the metal ion.
|
|
|
|
|
|
The above figures are
reprinted
by permission from John Wiley & Sons, Inc.:
Proteins
(2004,
54,
174-177)
copyright 2004.
|
|
|
|
|
|
|
