Phosphoribosylaminoimidazole carboxylase

Phosphoribosylaminoimidazole carboxylase (PurE) is part of the purine biosynthesis and catalyses the reversible conversion of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to 5-aminoimidazole ribonucleotide (AIR). In E. coli PurE is an independent enzyme while in plants and fungi it is a domain of phosphoribosylaminoimidazole carboxylase.

3D structures of PurE

Updated on 04-December-2013

1qcz – EcPurE – Escherichia coli

1o4v – PurE – Thermotoga maritima
1u11, 2fw1 - AaPurE – Acetobacter aceti
2fw6, 2fw7, 2fw8, 2fw9, 2fwa, 2fwb - AaPurE (mutant)
1xmp, 4ay3, 4ay4, 4b4k - PurE – Bacillus anthracis
2ywx – PurE – Methanocaldococcus jannaschii
3kuu - PurE (mutant) – Yersinia pestis
3lp6 - PurE (mutant) – Mycobacterium tuberculosis
3oow – FtPurE – Francesella tularensis
3rg8 – TdPurE – Treponema denticola
3trh – PurE – Coxiell burnetii
4ja0 – PurE – silkworm
3ors – PurE – Staphylococcus aureus
4grd – PurE – Burkholderia cenocepacia

PurE binary complex

2fwi, 2fwj - AaPurE (mutant) + AIR
1d7a – EcPurE + AIR
3rgg – TdPurE + AIR
2fwp - AaPurE (mutant) + iso-CAIR
2ate - EcPurE + nitro-AIR
2nsh - EcPurE (mutant) + nitro-AIR
2nsj, 2nsl - EcPurE (mutant) + CAIR
3opq – FtPurE + fructose-6-phosphate