 |
PDBsum entry 2gcu
|
|
|
|
References listed in PDB file
|
 |
|
Key reference
|
|
|
Title
|
|
Structure of an ethe1-Like protein from arabidopsis thaliana.
|
|
|
Authors
|
|
J.G.Mccoy,
C.A.Bingman,
E.Bitto,
M.M.Holdorf,
C.A.Makaroff,
G.N.Phillips.
|
|
|
Ref.
|
|
Acta Crystallogr D Biol Crystallogr, 2006,
62,
964-970.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
The protein product of gene At1g53580 from Arabidopsis thaliana possesses 54%
sequence identity to a human enzyme that has been implicated in the rare
disorder ethylmalonic encephalopathy. The structure of the At1g53580 protein has
been solved to a nominal resolution of 1.48 Angstrom. This structure reveals
tertiary structure differences between the ETHE1-like enzyme and glyoxalase II
enzymes that are likely to account for differences in reaction chemistry and
multimeric state between the two types of enzymes. In addition, the Arabidopsis
ETHE1 protein is used as a model to explain the significance of several
mutations in the human enzyme that have been observed in patients with
ethylmalonic encephalopathy.
|
|
|
|
|
|
|
|
Figure 1.
Figure 1 (a) The At1g53580 monomer. Helices are labelled 1-8
and  -strands
are labelled A-L. Residues known to be involved in human
ethylmalonic encephalopathy in human ETHE1 are colored pink. (b)
Overlay of the AtETHE1 (cyan) and the GLX2-5 (magenta) monomers.
The metal ions from the GLX2-5 structure are colored orange and
the iron ion from the AtETHE1 structure is colored gray. Arrows
point to changes between the folds of the two enzymes.
|
|
Figure 5.
Figure 5 Overlay of the substrate-binding residues from the
human glyoxalase II (cyan) with the equivalent residues in the
AtETHE1 enzyme (magenta). S-Hydroxybromophenylcarbamoyl
glutathione bound to glyoxalase II is colored yellow. Labels
correspond to AtETHE1.
|
|
|
|
|
|
The above figures are
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(2006,
62,
964-970)
copyright 2006.
|
|
|
|
|
|
|
