Abstract
A large volume of unexplained electron density in a crystal of N-acetyl-L-glutamate kinase (NAGK) is now interpreted as an external, very extended, metal-free AMPPNP molecule that occupies two alternative positions and that makes contacts with the protein exclusively through its gamma-imidophosphate. This external nucleotide is compared with the active-site nucleotide and the reasons for its extended shape, lack of complexed metal and peripheral binding are analyzed. Further, the possibility that this bystander AMPPNP is waiting to occupy the active centre is discussed.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callMore From: Acta Crystallographica Section D Biological Crystallography
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
