1T72

Crystal structure of phosphate transport system protein phoU from Aquifex aeolicus

Summary for 1T72

• Entry DOI: 10.2210/pdb1t72/pdb
• Descriptor: Phosphate transport system protein phoU homolog (2 entities in total)
• Functional Keywords: helix bundle, structural genomics, bsgc structure funded by nih, protein structure initiative, psi, berkeley structural genomics center, transport protein
• Biological source: Aquifex aeolicus
• Cellular location: Cytoplasm (By similarity): O67053
• Total number of polymer chains: 6
• Total formula weight: 158482.27

Authors

Oganesyan, V.,Kim, S.-H.,Oganesyan, N.,Jancarik, J.,Adams, P.D.,Kim, R.,Berkeley Structural Genomics Center (BSGC) (deposition date: 2004-05-07, release date: 2004-12-07, Last modification date: 2011-07-13)

Primary citation

Oganesyan, V.,Oganesyan, N.,Adams, P.D.,Jancarik, J.,Yokota, H.A.,Kim, R.,Kim, S.H.
Crystal structure of the "PhoU-like" phosphate uptake regulator from Aquifex aeolicus.
J.Bacteriol., 187:4238-4244, 2005

PubMed Abstract: The phoU gene of Aquifex aeolicus encodes a protein called PHOU_AQUAE with sequence similarity to the PhoU protein of Escherichia coli. Despite the fact that there is a large number of family members (more than 300) attributed to almost all known bacteria and despite PHOU_AQUAE's association with the regulation of genes for phosphate metabolism, the nature of its regulatory function is not well understood. Nearly one-half of these PhoU-like proteins, including both PHOU_AQUAE and the one from E. coli, form a subfamily with an apparent dimer structure of two PhoU domains on the basis of their amino acid sequence. The crystal structure of PHOU_AQUAE (a 221-amino-acid protein) reveals two similar coiled-coil PhoU domains, each forming a three-helix bundle. The structures of PHOU_AQUAE proteins from both a soluble fraction and refolded inclusion bodies (at resolutions of 2.8 and 3.2A, respectively) showed no significant differences. The folds of the PhoU domain and Bag domains (for a class of cofactors of the eukaryotic chaperone Hsp70 family) are similar. Accordingly, we propose that gene regulation by PhoU may occur by association of PHOU_AQUAE with the ATPase domain of the histidine kinase PhoR, promoting release of its substrate PhoB. Other proteins that share the PhoU domain fold include the coiled-coil domains of the STAT protein, the ribosome-recycling factor, and structural proteins like spectrin.

PubMed: 15937186
DOI: 10.1128/JB.187.12.4238-4244.2005

Experimental method

X-RAY DIFFRACTION (2.9 Å)