1.14.13.225: F-actin monooxygenase
This is an abbreviated version!
For detailed information about F-actin monooxygenase, go to the full flat file.
Word Map on EC 1.14.13.225
-
1.14.13.225
-
plexins
-
calponin
-
semaphorin-plexin
-
sema3a
-
plexa
-
semaphorin3a
-
rab8
- 1.14.13.225
-
plexins
- calponin
-
semaphorin-plexin
-
sema3a
- plexa
-
semaphorin3a
- rab8
Reaction
Synonyms
MICAL, MICAL-1, MICAL-2, MICAL1, Mical2, MICAL2PV, MICAL3
ECTree
Advanced search results
Crystallization
Crystallization on EC 1.14.13.225 - F-actin monooxygenase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
MICAL3 has an FAD/NADP-binding Rossmann-fold domain for monooxygenase activity. The flavin-containing monooxygenase (FMO) and calponin-homology (CH) domains of both MICAL3 and MICAL1 are highly similar in structure, but a different relative position of the calponin-homology domain in the asymmetric unit
purified recombinant His-tagged wild-type and mutant MICAL3 variants, sitting drop vapor diffusion method, method optimization, mixing of 500 nl of 25 mg/ml protein in 50 mM Tris, pH 8.5, 100 mM NaCl, 1 mM 1,4-dithiothreitol, 1% glycerol, with 500 nl of crystallization solution containing 0.1 M bicine-NaOH, pH 9.2, 7% v/v MPD, one day, X-ray diffraction structure determination and analysis at 1.9-2.3 A resolution
structure of a fragment of MICAL-1 containing the monooxygenase and the calponin homology domains. The calponin homology domain, loosely connected to the monooxygenase domain by a flexible linker and is far away from the catalytic site, couples F-actin to the enhancement of redox activity of MICALMO-CH by a cooperative mechanism involving a trans interaction between adjacently bound molecules