Abstract
When ATP binds to the active site of myosin heads, Switch II undergoes a large conformational change and the cleft surrounding the bound γ-phosphate closes. In the closed state, Glu470 in Switch II comes together with Arg247 in Switch I to form a salt-bridge. Here, the functional significance of the two bridging residues was tested by using site-directed mutagenesis. We conclude from such tests that (a) the attractive force between Arg247 and the γ-phosphate of ATP moves the cleft to close, and (b) during hydrolysis, Glu470 is intimately involved in positioning the lytic water for the attack on the γ-phosphorus. We also speculate on how the salt-bridge between Arg247 and Glu470 is related to hydrolysis.
| Original language | English |
|---|---|
| Pages (from-to) | 175-181 |
| Number of pages | 7 |
| Journal | Advances in Experimental Medicine and Biology |
| Volume | 538 |
| Publication status | Published - 2004 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
Cite this
A hypothesis about myosin catalysis. / Onishi, Hirofumi; Ohki, Takashi; Mozhizuki, Naoki; Morales, Manuel F.
In: Advances in Experimental Medicine and Biology, Vol. 538, 2004, p. 175-181.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - A hypothesis about myosin catalysis
AU - Onishi, Hirofumi
AU - Ohki, Takashi
AU - Mozhizuki, Naoki
AU - Morales, Manuel F.
PY - 2004
Y1 - 2004
N2 - When ATP binds to the active site of myosin heads, Switch II undergoes a large conformational change and the cleft surrounding the bound γ-phosphate closes. In the closed state, Glu470 in Switch II comes together with Arg247 in Switch I to form a salt-bridge. Here, the functional significance of the two bridging residues was tested by using site-directed mutagenesis. We conclude from such tests that (a) the attractive force between Arg247 and the γ-phosphate of ATP moves the cleft to close, and (b) during hydrolysis, Glu470 is intimately involved in positioning the lytic water for the attack on the γ-phosphorus. We also speculate on how the salt-bridge between Arg247 and Glu470 is related to hydrolysis.
AB - When ATP binds to the active site of myosin heads, Switch II undergoes a large conformational change and the cleft surrounding the bound γ-phosphate closes. In the closed state, Glu470 in Switch II comes together with Arg247 in Switch I to form a salt-bridge. Here, the functional significance of the two bridging residues was tested by using site-directed mutagenesis. We conclude from such tests that (a) the attractive force between Arg247 and the γ-phosphate of ATP moves the cleft to close, and (b) during hydrolysis, Glu470 is intimately involved in positioning the lytic water for the attack on the γ-phosphorus. We also speculate on how the salt-bridge between Arg247 and Glu470 is related to hydrolysis.
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UR - http://www.scopus.com/inward/citedby.url?scp=1842474954&partnerID=8YFLogxK
M3 - Article
C2 - 15098665
AN - SCOPUS:1842474954
VL - 538
SP - 175
EP - 181
JO - Advances in Experimental Medicine and Biology
JF - Advances in Experimental Medicine and Biology
SN - 0065-2598
ER -