Stabilization of the ADP/metaphosphate intermediate during ATP hydrolysis in pre-power stroke myosin: quantitative anatomy of an enzyme
It has been proposed recently that ATP hydrolysis in ATPase enzymes proceeds via an initial intermediate in which the dissociated γ-phosphate of ATP is bound in the protein as a metaphosphate (PγO3−). A combined quantum/classical analysis of this dissociated nucleotide state inside myosin provides a...
Gespeichert in:
| Hauptverfasser: | , |
|---|---|
| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
October 28, 2013
|
| In: |
JBC papers in press
Year: 2013, Jahrgang: 288, Heft: 49, Pages: 35569-35580 |
| DOI: | 10.1074/jbc.M113.500298 |
| Online-Zugang: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1074/jbc.M113.500298 Verlag, lizenzpflichtig, Volltext: https://www.sciencedirect.com/science/article/pii/S0021925820554197 
|
| Verfasserangaben: | Farooq Ahmad Kiani and Stefan Fischer |
MARC
| LEADER | 00000caa a2200000 c 4500 | ||
|---|---|---|---|
| 001 | 1753284856 | ||
| 003 | DE-627 | ||
| 005 | 20230426165449.0 | ||
| 007 | cr uuu---uuuuu | ||
| 008 | 210407s2013 xx |||||o 00| ||eng c | ||
| 024 | 7 | |a 10.1074/jbc.M113.500298 |2 doi | |
| 035 | |a (DE-627)1753284856 | ||
| 035 | |a (DE-599)KXP1753284856 | ||
| 035 | |a (OCoLC)1341403677 | ||
| 040 | |a DE-627 |b ger |c DE-627 |e rda | ||
| 041 | |a eng | ||
| 084 | |a 30 |2 sdnb | ||
| 100 | 1 | |a Kiani, Farooq Ahmad |e VerfasserIn |0 (DE-588)132274280 |0 (DE-627)520398785 |0 (DE-576)258672374 |4 aut | |
| 245 | 1 | 0 | |a Stabilization of the ADP/metaphosphate intermediate during ATP hydrolysis in pre-power stroke myosin |b quantitative anatomy of an enzyme |c Farooq Ahmad Kiani and Stefan Fischer |
| 264 | 1 | |c October 28, 2013 | |
| 300 | |a 12 | ||
| 336 | |a Text |b txt |2 rdacontent | ||
| 337 | |a Computermedien |b c |2 rdamedia | ||
| 338 | |a Online-Ressource |b cr |2 rdacarrier | ||
| 500 | |a Gesehen am 07.04.2021 | ||
| 520 | |a It has been proposed recently that ATP hydrolysis in ATPase enzymes proceeds via an initial intermediate in which the dissociated γ-phosphate of ATP is bound in the protein as a metaphosphate (PγO3−). A combined quantum/classical analysis of this dissociated nucleotide state inside myosin provides a quantitative understanding of how the enzyme stabilizes this unusual metaphosphate. Indeed, in vacuum, the energy of the ADP3−·PγO3−·Mg2+ complex is much higher than that of the undissociated ATP4−. The protein brings it to a surprisingly low value. Energy decomposition reveals how much each interaction in the protein stabilizes the metaphosphate state; backbone peptides of the P-loop contribute 50% of the stabilization energy, and the side chain of Lys-185+ contributes 25%. This can be explained by the fact that these groups make strong favorable interactions with the α- and β-phosphates, thus favoring the charge distribution of the metaphosphate state over that of the ATP state. Further stabilization (16%) is achieved by a hydrogen bond between the backbone C=O of Ser-237 (on loop Switch-1) and a water molecule perfectly positioned to attack the PγO3− in the subsequent hydrolysis step. The planar and singly negative PγO3− is a much better target for the subsequent nucleophilic attack by a negatively charged OH− than the tetrahedral and doubly negative PγO42− group of ATP. Therefore, we argue that the present mechanism of metaphosphate stabilization is common to the large family of nucleotide-hydrolyzing enzymes. Methodologically, this work presents a computational approach that allows us to obtain a truly quantitative conception of enzymatic strategy. | ||
| 650 | 4 | |a ATP | |
| 650 | 4 | |a ATPases | |
| 650 | 4 | |a Bioenergetics | |
| 650 | 4 | |a Biophysics | |
| 650 | 4 | |a Computational Biology | |
| 650 | 4 | |a Computer Modeling | |
| 650 | 4 | |a Enzyme Catalysis | |
| 650 | 4 | |a Enzyme Mechanisms | |
| 650 | 4 | |a Myosin | |
| 650 | 4 | |a Quantum Chemistry | |
| 700 | 1 | |a Fischer, Stefan |e VerfasserIn |0 (DE-588)1026232961 |0 (DE-627)726307378 |0 (DE-576)371534100 |4 aut | |
| 773 | 0 | 8 | |i Enthalten in |t JBC papers in press |d Bethesda, MD : American Soc. for Biochemistry and Molecular Biology, 2003 |g 288(2013), 49, Seite 35569-35580 |h Online-Ressource |w (DE-627)385029187 |w (DE-600)2141744-1 |w (DE-576)34726901X |7 nnas |a Stabilization of the ADP/metaphosphate intermediate during ATP hydrolysis in pre-power stroke myosin quantitative anatomy of an enzyme |
| 773 | 1 | 8 | |g volume:288 |g year:2013 |g number:49 |g pages:35569-35580 |g extent:12 |a Stabilization of the ADP/metaphosphate intermediate during ATP hydrolysis in pre-power stroke myosin quantitative anatomy of an enzyme |
| 856 | 4 | 0 | |u https://doi.org/10.1074/jbc.M113.500298 |x Verlag |x Resolving-System |z lizenzpflichtig |3 Volltext |
| 856 | 4 | 0 | |u https://www.sciencedirect.com/science/article/pii/S0021925820554197 |x Verlag |z lizenzpflichtig |3 Volltext |
| 951 | |a AR | ||
| 992 | |a 20210407 | ||
| 993 | |a Article | ||
| 994 | |a 2013 | ||
| 998 | |g 1026232961 |a Fischer, Stefan |m 1026232961:Fischer, Stefan |d 700000 |d 708000 |e 700000PF1026232961 |e 708000PF1026232961 |k 0/700000/ |k 1/700000/708000/ |p 2 |y j | ||
| 998 | |g 132274280 |a Kiani, Farooq Ahmad |m 132274280:Kiani, Farooq Ahmad |p 1 |x j | ||
| 999 | |a KXP-PPN1753284856 |e 390314116X | ||
| BIB | |a Y | ||
| SER | |a journal | ||
| JSO | |a {"origin":[{"dateIssuedKey":"2013","dateIssuedDisp":"October 28, 2013"}],"id":{"doi":["10.1074/jbc.M113.500298"],"eki":["1753284856"]},"name":{"displayForm":["Farooq Ahmad Kiani and Stefan Fischer"]},"physDesc":[{"extent":"12 S."}],"relHost":[{"title":[{"title_sort":"JBC papers in press","title":"JBC papers in press"}],"titleAlt":[{"title":"Papers in press"}],"part":{"issue":"49","pages":"35569-35580","year":"2013","extent":"12","text":"288(2013), 49, Seite 35569-35580","volume":"288"},"pubHistory":["2003,May -"],"recId":"385029187","language":["eng"],"note":["Gesehen am 23.06.21"],"disp":"Stabilization of the ADP/metaphosphate intermediate during ATP hydrolysis in pre-power stroke myosin quantitative anatomy of an enzymeJBC papers in press","type":{"media":"Online-Ressource","bibl":"periodical"},"id":{"zdb":["2141744-1"],"eki":["385029187"]},"origin":[{"dateIssuedDisp":"2003-","publisher":"American Soc. for Biochemistry and Molecular Biology","dateIssuedKey":"2003","publisherPlace":"Bethesda, MD"}],"physDesc":[{"extent":"Online-Ressource"}]}],"title":[{"title_sort":"Stabilization of the ADP/metaphosphate intermediate during ATP hydrolysis in pre-power stroke myosin","subtitle":"quantitative anatomy of an enzyme","title":"Stabilization of the ADP/metaphosphate intermediate during ATP hydrolysis in pre-power stroke myosin"}],"person":[{"role":"aut","roleDisplay":"VerfasserIn","display":"Kiani, Farooq Ahmad","given":"Farooq Ahmad","family":"Kiani"},{"family":"Fischer","given":"Stefan","roleDisplay":"VerfasserIn","display":"Fischer, Stefan","role":"aut"}],"type":{"bibl":"article-journal","media":"Online-Ressource"},"note":["Gesehen am 07.04.2021"],"language":["eng"],"recId":"1753284856"} | ||
| SRT | |a KIANIFAROOSTABILIZAT2820 | ||