1t72

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(New page: 200px<br /><applet load="1t72" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t72, resolution 2.9&Aring;" /> '''Crystal structure of ...)
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Revision as of 00:54, 21 November 2007


1t72, resolution 2.9Å

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Crystal structure of phosphate transport system protein phoU 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

1T72 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

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