1t8b: Difference between revisions
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{{STRUCTURE_1t8b| PDB=1t8b | SCENE= }} | |||
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'''Crystal structure of refolded PHOU-like protein (gi 2983430) from Aquifex aeolicus''' | '''Crystal structure of refolded PHOU-like protein (gi 2983430) from Aquifex aeolicus''' | ||
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[[Category: Oganesyan, N.]] | [[Category: Oganesyan, N.]] | ||
[[Category: Oganesyan, V.]] | [[Category: Oganesyan, V.]] | ||
[[Category: | [[Category: Alpha-helical protein consisting of two 3-helix bundle]] | ||
[[Category: | [[Category: Berkeley structural genomics center]] | ||
[[Category: | [[Category: Bsgc structure funded by nih]] | ||
[[Category: | [[Category: Protein structure initiative]] | ||
[[Category: | [[Category: Psi]] | ||
[[Category: | [[Category: Structural genomic]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:39:42 2008'' | |||
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Revision as of 06:39, 3 May 2008
Crystal structure of refolded PHOU-like protein (gi 2983430) from Aquifex aeolicus
Overview
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.
About this Structure
1T8B is a Single protein structure of sequence from Aquifex aeolicus. Full crystallographic information is available from OCA.
Reference
Crystal structure of the "PhoU-like" phosphate uptake regulator from Aquifex aeolicus., Oganesyan V, Oganesyan N, Adams PD, Jancarik J, Yokota HA, Kim R, Kim SH, J Bacteriol. 2005 Jun;187(12):4238-44. PMID:15937186 Page seeded by OCA on Sat May 3 09:39:42 2008
Proteopedia Page Contributors and Editors (what is this?)
- Pages with broken file links
- Aquifex aeolicus
- Single protein
- Adams, P D.
- BSGC, Berkeley Structural Genomics Center.
- Jancarik, J.
- Kim, R.
- Kim, S H.
- Oganesyan, N.
- Oganesyan, V.
- Alpha-helical protein consisting of two 3-helix bundle
- Berkeley structural genomics center
- Bsgc structure funded by nih
- Protein structure initiative
- Psi
- Structural genomic
