This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


Nucleoside triphosphatase

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (06:42, 22 August 2023) (edit) (undo)
 
(23 intermediate revisions not shown.)
Line 1: Line 1:
-
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
 
-
10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
 
 +
<StructureSection load='4a5a' size='350' side='right' caption='NTPase 2 tetramer complex with AMPPNP and Mg++ ion (green) (PDB entry [[4a5a]])' scene=''>
== Function ==
== Function ==
-
'''Nucleoside triphosphatase''' or '''nucleoside triphosphate diphosphohydrolase''' (NTPase)
+
'''Nucleoside triphosphatase''' or '''nucleoside triphosphate diphosphohydrolase''' (NTPase) is responsible for degradation of nucleotides to their monophosphate form. NTPase is found in mammals and in pathogenic microbes. In mammals NTPase hs a crucial role in regulation of purinergic signalling by hydrolysis of extracellular nucleotides. The function of NTPase in pathogens is still unknown<ref>PMID:24115522</ref>.
-
 
+
-
== Disease ==
+
== Relevance ==
== Relevance ==
 +
 +
The modulation of NTPase activity sems a good therapeutic method for regulating the concentration of ATP. High ATP concentration has been shown to be involved in various disorders in the CNS including brain injury, ischemia, neuro-inflammation, epilepsy, neuropathic pain and migraine<ref>PMID:25694082</ref>.
== Structural highlights ==
== Structural highlights ==
 +
''Toxoplasma gondii'' <snapshot name='84/844927/Cv1/3'>NTPase 2 is dimer of dimers</snapshot> (PDB code [[4a5a]]). The 3D structure of the complex between NTPase 2 and the ATP analog AMPPNP shows the NTPase structure composed of two domains. Domain I contains the N-terminal and C-terminal and domain II the core residues. 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>.
 +
*<snapshot name='84/844927/Cv1/5'>Test1</snapshot>
 +
*<snapshot name='84/844927/Cv1/6'>Test2</snapshot>
 +
*<snapshot name='84/844927/Cv1/8'>Test3</snapshot>
-
 
+
</SX>
-
</StructureSection>
+
==3D structures of nucleoside triphosphatase==
==3D structures of nucleoside triphosphatase==
Line 36: Line 38:
**[[6dt3]] - Nudi - ''Klebsiella pneumoniae'' <br />
**[[6dt3]] - Nudi - ''Klebsiella pneumoniae'' <br />
 +
**[[3oga]], [[3n77]] - Nudi - ''Salmonella enterica'' <br />
*Nucleoside triphosphatase cancer-related
*Nucleoside triphosphatase cancer-related
Line 44: Line 47:
**[[3s86]] - NTPase - ''Thermotoga maritima'' <br />
**[[3s86]] - NTPase - ''Thermotoga maritima'' <br />
-
 
+
**[[3agr]] - NTPase - ''Neospora caninum'' <br />
 +
**[[7aoh]] - NTPase I in transcribing complex - Vaccinia virus – Cryo EM <br />
 +
}}
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

NTPase 2 tetramer complex with AMPPNP and Mg++ ion (green) (PDB entry 4a5a)

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

Alexander Berchansky, Michal Harel, Joel L. Sussman

Personal tools