THE AWD NUCLEOTIDE DIPHOSPHATE KINASE FROM DROSOPHILATHE AWD NUCLEOTIDE DIPHOSPHATE KINASE FROM DROSOPHILA

Structural highlights

1ndl is a 3 chain structure with sequence from Drome. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Activity:Nucleoside-diphosphate kinase, with EC number 2.7.4.6
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[NDKA_DROME] Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.[1] [2] [3]

Evolutionary Conservation

 

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

BACKGROUND: Nucleotide diphosphate kinase (NDP kinase) is a phosphate transfer enzyme involved in cell regulation and in animal development. Drosophila NDP kinase is the product of the abnormal wing disc (awd) developmental gene, a point mutation in which can produce the killer of prune (K-pn) conditional lethal phenotype. The highly homologous mammalian genes control metastasis and a human NDP kinase acts as a transcription factor. RESULTS: The X-ray structure of the Awd protein prepared from Drosophila was solved at 2.4 A resolution by molecular replacement from the homologous Dictyostelium protein. Both are hexamers, and both have the same fold and the same active site. Subunit contacts differ as a result of sequence changes in the carboxy-terminal segment and in the loop that is the site of the K-pn mutation. CONCLUSIONS: Regulatory properties of animal NDP kinases depend on interactions with other macromolecules, such as DNA and the product of the Drosophila prune gene. The Awd structure suggests an allosteric mechanism of action of NDP kinase where DNA is the effector and the protein undergoes a major conformational change, possibly dissociating to dimers.

Crystal structure of the Awd nucleotide diphosphate kinase from Drosophila.,Chiadmi M, Morera S, Lascu I, Dumas C, Le Bras G, Veron M, Janin J Structure. 1993 Dec 15;1(4):283-93. PMID:8081741[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Biggs J, Tripoulas N, Hersperger E, Dearolf C, Shearn A. Analysis of the lethal interaction between the prune and Killer of prune mutations of Drosophila. Genes Dev. 1988 Oct;2(10):1333-43. PMID:2849580
  2. Biggs J, Hersperger E, Steeg PS, Liotta LA, Shearn A. A Drosophila gene that is homologous to a mammalian gene associated with tumor metastasis codes for a nucleoside diphosphate kinase. Cell. 1990 Nov 30;63(5):933-40. PMID:2175255
  3. Timmons L, Xu J, Hersperger G, Deng XF, Shearn A. Point mutations in awdKpn which revert the prune/Killer of prune lethal interaction affect conserved residues that are involved in nucleoside diphosphate kinase substrate binding and catalysis. J Biol Chem. 1995 Sep 29;270(39):23021-30. PMID:7559441
  4. Chiadmi M, Morera S, Lascu I, Dumas C, Le Bras G, Veron M, Janin J. Crystal structure of the Awd nucleotide diphosphate kinase from Drosophila. Structure. 1993 Dec 15;1(4):283-93. PMID:8081741

1ndl, resolution 2.40Å

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