| Autor: |
Drum CL; Committee on Neurobiology, The University of Chicago, 924 East 57th Street, Chicago, IL 60637, USA., Shen Y, Rice PA, Bohm A, Tang WJ |
| Jazyk: |
angličtina |
| Zdroj: |
Acta crystallographica. Section D, Biological crystallography [Acta Crystallogr D Biol Crystallogr] 2001 Dec; Vol. 57 (Pt 12), pp. 1881-4. Date of Electronic Publication: 2001 Nov 21. |
| DOI: |
10.1107/s0907444901014937 |
| Abstrakt: |
Edema factor from Bacillus anthracis is a 92 kDa secreted adenylyl cyclase exotoxin and is activated by the host-resident protein calmodulin. Calmodulin is a ubiquitous intracellular calcium sensor in eukaryotes and activates edema factor nearly 1000-fold upon binding. While calmodulin has many known effectors, including kinases, phosphodiesterases, motor proteins, channels and type 1 adenylyl cyclases, no structures of calmodulin in complex with a functional enzyme have been solved. The crystallization and initial experimental phasing of crystals containing a complex of edema factor adenylyl cyclase domain and calmodulin are reported here. The edema factor-calmodulin complex crystallizes in three different space groups. A native data set in the I222 space group has been collected to 2.7 A and the self-rotation function solution suggests three edema factor-calmodulin complexes in each asymmetric unit. Initial 4 A phases were obtained by selenomethionyl MAD in combination with two heavy-atom derivatives. These phases were successfully extended to 2.7 A using NCS averaging. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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