1DK4

CRYSTAL STRUCTURE OF MJ0109 GENE PRODUCT INOSITOL MONOPHOSPHATASE

Summary for 1DK4

• Entry DOI: 10.2210/pdb1dk4/pdb
• Related: 1awb
• Descriptor: INOSITOL MONOPHOSPHATASE, ZINC ION, PHOSPHATE ION, ... (4 entities in total)
• Functional Keywords: homodimer, complexed with zn and pi, hydrolase
• Biological source: Methanocaldococcus jannaschii
• Total number of polymer chains: 2
• Total formula weight: 57806.07

Authors

Stec, B.,Yang, H.,Johnson, K.A.,Chen, L.,Roberts, M.F. (deposition date: 1999-12-06, release date: 2000-11-08, Last modification date: 2023-08-09)

Primary citation

Stec, B.,Yang, H.,Johnson, K.A.,Chen, L.,Roberts, M.F.
MJ0109 is an enzyme that is both an inositol monophosphatase and the 'missing' archaeal fructose-1,6-bisphosphatase.
Nat.Struct.Biol., 7:1046-1050, 2000

PubMed Abstract: In sequenced genomes, protein coding regions with unassigned function constitute between 10 and 50% of all open reading frames. Often key enzymes cannot be identified using sequence homology searches. For example, despite the fact that methanogens have an apparently functional gluconeogenesis pathway, standard tools have been unable to identify a fructose-1,6-bisphosphatase (FBPase) gene in the sequenced Methanoccocus jannaschii genome. Using a combination of functional and structural tools, we have shown that the protein product of the M. jannaschii gene MJ0109, which had been tentatively annotated as an inositol monophosphatase (IMPase), has both IMPase and FBPase activities. Moreover, several gene products annotated as IMPases from different thermophilic organisms also possess FBPase activity. Thus, we have found the FBPase that was 'missing' in thermophiles and shown that it also functions as an IMPase.

PubMed: 11062561
DOI: 10.1038/80968

Experimental method

X-RAY DIFFRACTION (2.6 Å)