This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1t72

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1t72.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1t72.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1t72| PDB=1t72 | SCENE= }}
{{STRUCTURE_1t72| PDB=1t72 | SCENE= }}
-
'''Crystal structure of phosphate transport system protein phoU from Aquifex aeolicus'''
+
===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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15937186}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15937186 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15937186}}
==About this Structure==
==About this Structure==
Line 35: Line 39:
[[Category: Psi]]
[[Category: Psi]]
[[Category: Structural genomic]]
[[Category: Structural genomic]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:36:51 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 14:34:21 2008''

Revision as of 11:34, 27 July 2008

Image:1t72.png

Template:STRUCTURE 1t72

Crystal structure of phosphate transport system protein phoU from Aquifex aeolicus

Template:ABSTRACT PUBMED 15937186

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

Page seeded by OCA on Sun Jul 27 14:34:21 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1t72"
Personal tools