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Nucleoside triphosphatase
From Proteopedia
(Difference between revisions)
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| - | <StructureSection load='4a5a' size='340' side='right' caption=' | + | <StructureSection load='4a5a' size='340' side='right' caption='NTPase 2 tetramer complex with AMPPNP and Mg++ ion (green) (PDB code [[4a5a]])' scene=''> |
== Function == | == Function == | ||
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== Structural highlights == | == Structural highlights == | ||
| - | + | The 3D structure of the complex between NTPase 2 and the ATP analog AMPPNP shows the NTPase structure composed of two domains. The structure contains 7 Cys-Cys bonds one of which located between domain I and II and reaching the diametrically positioned monomer was found by mutational analysis to be responsible for activation. The ATP analog - AMPPNP - is located in a cleft and forms interactions with domain I and domain II<ref>PMID:22130673</ref>. | |
</StructureSection> | </StructureSection> | ||
Revision as of 08:19, 12 May 2020
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3D structures of nucleoside triphosphatase
Updated on 12-May-2020
References
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
- ↑ Krug U, Zebisch M, Krauss M, Strater N. Structural insight into the activation mechanism of Toxoplasma gondii nucleoside triphosphate diphosphohydrolases by disulfide reduction. J Biol Chem. 2011 Nov 30. PMID:22130673 doi:10.1074/jbc.M111.294348
