Acta Crystallogr D Biol Crystallogr. 2002 Oct;58(Pt 10 Pt 2):1892-5. Epub 2002 Sep 28.

A crystallographic glimpse of a nucleotide triphosphate (AMPPNP) bound to a protein surface: external and internal AMPPNP molecules in crystalline N-acetyl-L-glutamate kinase.

Gil-Ortiz F, Fita I, Ramón-Maiques S, Marina A, Rubio V.

Source

Instituto de Biomedicina de Valencia, Consejo Superior de Investigaciones Científicas (IBV-CSIC), C/Jaime Roig 11, 46010-Valencia, Spain.

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.

PMID:: 12351849; [PubMed - indexed for MEDLINE]

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Research Support, Non-U.S. Gov't

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PDB/1GS5

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A crystallographic glimpse of a nucleotide triphosphate (AMPPNP) bound to a prot...
A crystallographic glimpse of a nucleotide triphosphate (AMPPNP) bound to a protein surface: external and internal AMPPNP molecules in crystalline N-acetyl-L-glutamate kinase.
Acta Crystallogr D Biol Crystallogr. 2002 Oct ;58(Pt 10 Pt 2):1892-5. Epub 2002 Sep 28 .

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