1EMS

CRYSTAL STRUCTURE OF THE C. ELEGANS NITFHIT PROTEIN

Summary for 1EMS

• Entry DOI: 10.2210/pdb1ems/pdb
• Descriptor: NIT-FRAGILE HISTIDINE TRIAD FUSION PROTEIN, ETHYL MERCURY ION, SODIUM ION, ... (5 entities in total)
• Functional Keywords: worm, nitrilase, fhit, nucleotide-binding protein, cancer, diadenosine polyphosphate hydrolase, histidine triad, tumor suppressor, rosetta stone, antitumor protein
• Biological source: Caenorhabditis elegans
• Total number of polymer chains: 2
• Total formula weight: 101374.28

Authors

Pace, H.C.,Hodawadekar, S.C.,Draganescu, A.,Huang, J.,Bieganowski, P.,Pekarsky, Y.,Croce, C.M.,Brenner, C. (deposition date: 2000-03-17, release date: 2000-07-20, Last modification date: 2024-02-07)

Primary citation

Pace, H.C.,Hodawadekar, S.C.,Draganescu, A.,Huang, J.,Bieganowski, P.,Pekarsky, Y.,Croce, C.M.,Brenner, C.
Crystal structure of the worm NitFhit Rosetta Stone protein reveals a Nit tetramer binding two Fhit dimers.
Curr.Biol., 10:907-917, 2000

PubMed Abstract: The nucleotide-binding protein Fhit, among the earliest and most frequently inactivated proteins in lung cancer, suppresses tumor formation by inducing apoptosis. In invertebrates, Fhit is encoded as a fusion protein with Nit, a member of the nitrilase superfamily. In mice, the Nit1 and Fhit genes have nearly identical expression profiles. According to the Rosetta Stone hypothesis, if the separate Nit and Fhit genes could be shown to occur in the same subset of genomes (that is, to share a phylogenetic profile), then the existence of a fusion protein in invertebrates and the coordinated expression of separate mRNAs in mouse suggest that Nit and Fhit function in the same pathway and that the structure of invertebrate NitFhit may reflect the nature of Nit-Fhit interactions.

PubMed: 10959838
DOI: 10.1016/S0960-9822(00)00621-7

Experimental method

X-RAY DIFFRACTION (2.8 Å)