Acta Crystallographica Section D
Acta Crystallographica
Section D
STRUCTURAL BIOLOGY
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Acta Cryst.
(2014).
D
70
,
2101-2110
https://doi.org/10.1107/S1399004714012140
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Domain mobility as probed by small-angle X-ray scattering may account for substrate access to the active site of two copper-dependent amine oxidases
E. Dainese
,
A. Sabatucci
,
F. Pintus
,
R. Medda
,
C. B. Angelucci
,
G. Floris
and
M. Maccarrone
SAXS analysis suggests that in solution CAOs homodimers could undergo a conformational change. The D3 domain seems to move with respect to the rest of the protein, increasing the accessibility of the active site.
Keywords:
amine oxidase
;
SAXS
;
copper
;
TPQ
;
TOPA
;
conformational change
;
domain movement
.
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