Structural highlights
Function
[PHOU2_THEMA] Plays a role in the regulation of phosphate uptake (By similarity).
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
PhoU proteins are known to play a role in the regulation of phosphate uptake. In Thermotoga maritima, two PhoU homologues have been identified bioinformatically. Here we report the crystal structure of one of the PhoU homologues at 2.0 A resolution. The structure of the PhoU protein homologue contains a highly symmetric new structural fold composed of two repeats of a three-helix bundle. The structure unexpectedly revealed a trinuclear and a tetranuclear iron cluster that were found to be bound on the surface. Each of the two multinuclear iron clusters is coordinated by a conserved E(D)XXXD motif pair. Our structure reveals a new class of metalloprotein containing multinuclear iron clusters. The possible functional implication based on the structure are discussed.
Crystal structure of a PhoU protein homologue: a new class of metalloprotein containing multinuclear iron clusters.,Liu J, Lou Y, Yokota H, Adams PD, Kim R, Kim SH J Biol Chem. 2005 Apr 22;280(16):15960-6. Epub 2005 Feb 16. PMID:15716271[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Liu J, Lou Y, Yokota H, Adams PD, Kim R, Kim SH. Crystal structure of a PhoU protein homologue: a new class of metalloprotein containing multinuclear iron clusters. J Biol Chem. 2005 Apr 22;280(16):15960-6. Epub 2005 Feb 16. PMID:15716271 doi:10.1074/jbc.M414117200
