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PDBsum entry 1i9c
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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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Radical shuttling in a protein: ribose pseudorotation controls alkyl-Radical transfer in the coenzyme b(12) dependent enzyme glutamate mutase this work was supported by the österreichische akademie der wissenschaften (apart fellowship 614), The österreichische fonds zur förderung der wissenschaftlichen forschung (fwf-Project 11599), And the european commission (tmr project number erb 4061 pl 95-0307). Crystallographic data were collected at the embl-Beamline bw7b at desy in hamburg, Germany. We thank the beamline scientists for their assistance, And ingrid dreveny, Günter gartler, Gerwald jogl, And oliver sauer for their help during data collection. This research emerged from a collaboration with prof. W. Buckel (marburg) who supplied us with clones of the glutamate mutase proteins.
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Authors
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K.Gruber,
R.Reitzer,
C.Kratky.
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Ref.
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Angew Chem Int Ed Engl, 2001,
40,
3377-3380.
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PubMed id
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Abstract
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No abstract given.
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Secondary reference #1
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Title
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Glutamate mutase from clostridum cochlearium: the structure of a coenzyme b12-Dependent enzyme provides new mechanistic insights
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Authors
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R.Reitzer,
K.Gruber,
G.Jogl,
U.G.Wagner,
H.Bothe,
W.Buckel,
C.Kratky.
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Ref.
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structure, 1999,
7,
891.
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Secondary reference #2
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Title
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Crystallization and preliminary X-Ray analysis of recombinant glutamate mutase and of the isolated component s from clostridium cochlearium.
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Authors
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R.Reitzer,
M.Krasser,
G.Jogl,
W.Buckel,
H.Bothe,
C.Kratky.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 1998,
54,
1039-1042.
[DOI no: ]
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PubMed id
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Figure 1.
Fig. 1. ata collection (EMBL beamline Xll, DESY, Hamburg) on
component S with cyanocobalamin. Exposure time 4 min, oscilla-
tion range 1.0 °.
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Figure 3.
Fig. 3 Self-rotation function h~r component S with cyanocobalamin. A
section at x = 18ff is show. Data btween a resoltion of 10 and
4 A were used, integration radius 25 A. Contouring started at 15%
in 5% increments. The axis conventions are as follows: ~c is the
rotation axis whose orientation with respect to the (orthogonalized)
axes is defined by ~) (angle from z axis) and ~0 (angle in the x, y
plane).
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The above figures are
reproduced from the cited reference
with permission from the IUCr
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Secondary reference #3
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Title
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Characterization of the coenzyme-B12-Dependent glutamate mutase from clostridium cochlearium produced in escherischia coli
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Authors
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O.Zelder,
B.Beatrix,
U.Leutbecher,
W.Buckel.
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Ref.
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eur j biochem, 1994,
226,
577.
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