NDLI: Backbone and side-chain resonance assignments of Plasmodium falciparum SUMO

Content Provider	Springer Nature Link
Author	Singh, Jai Shankar Shukla, Vaibhav Kumar Gujrati, Mansi Mishra, Ram Kumar Kumar, Ashutosh
Copyright Year	2016
Abstract	One of the most debilitating diseases Malaria, in its different forms, is caused by protozoan of Plasmodium species. Deadliest among these forms is the “cerebral malaria” which is afflicted upon by Plasmodium falciparum. Plasmodium adopts numerous strategies including various post-translational modifications (PTMs) to infect and survive in the human host. These PTMs have proven their critical requirement in the Plasmodium biology. Recently, sumoylation has been characterized as one of the important PTMs and many of its putative substrates have been identified in Plasmodium. Sumoylation is the covalent attachment of SUMO protein to the substrate protein, which is mediated by an enzyme cascade involving activating (E1), conjugating (E2), and ligating enzymes (E3). Here, we report resonance assignment for $^{1}$H, $^{13}$C and $^{15}$N of Plasmodium falciparum SUMO (Pf-SUMO) protein determined by various 2D and 3D heteronuclear NMR experiments along with predicted secondary structures.
Starting Page	17
Ending Page	20
Page Count	4
File Format	PDF
ISSN	18742718
Journal	Biomolecular NMR Assignments
Volume Number	11
Issue Number	1
e-ISSN	1874270X
Language	English
Publisher	Springer Netherlands
Publisher Date	2016-10-03
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Sumoylation NMR Resonance assignment Pf-SUMO Biological and Medical Physics, Biophysics Polymer Sciences Biochemistry
Content Type	Text
Resource Type	Article
Subject	Structural Biology Biochemistry

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