2jba

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2jba.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2jba.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2jba| PDB=2jba | SCENE= }}
{{STRUCTURE_2jba| PDB=2jba | SCENE= }}
-
'''PHOB RESPONSE REGULATOR RECEIVER DOMAIN CONSTITUTIVELY-ACTIVE DOUBLE MUTANT D53A AND Y102C.'''
+
===PHOB RESPONSE REGULATOR RECEIVER DOMAIN CONSTITUTIVELY-ACTIVE DOUBLE MUTANT D53A AND Y102C.===
-
==Overview==
+
<!--
-
The PhoR/PhoB two-component system is a key regulatory protein network enabling Escherichia coli to respond to inorganic phosphate (Pi) starvation conditions by turning on Pho regulon genes for more efficient Pi uptake and use of alternative phosphorus sources. Under environmental Pi depletion, the response regulator (RR) component, PhoB, is phosphorylated at the receiver domain (RD), a process that requires Mg(2+) bound at the active site. Phosphorylation of the RD relieves the inhibition of the PhoB effector domain (ED), a DNA-binding region that binds to Pho regulon promoters to activate transcription. The molecular details of the activation are proposed to involve dimerization of the RD and a conformational change in the RD detected by the ED. The structure of the PhoB RD shows a symmetrical interaction involving alpha1, loop beta5alpha5 and N terminus of alpha5 elements, also seen in the complex of PhoB RD with Mg(2+), in which helix alpha4 highly increases its flexibility. PhoB RD in complex with Mg(2+) and BeF(3) (an emulator of the phosphate moiety) undergoes a dramatic conformational change on helix alpha4 and shows another interaction involving alpha4, beta5 and alpha5 segments. We have selected a series of constitutively active PhoB mutants (PhoB(CA)) that are able to turn on the Pho regulon promoters in the absence phosphorylation and, as they cannot be inactivated, should therefore mimic the active RD state of PhoB and its functional oligomerisation. We have analysed the PhoB(CA) RD crystal structures of two such mutants, Asp53Ala/Tyr102Cys and Asp10Ala/Asp53Glu. Interestingly, both mutants reproduce the homodimeric arrangement through the symmetric interface encountered in the unbound and magnesium-bound wild-type PhoB RD structures. Besides, the mutant RD structures show a modified active site organization as well as changes at helix alpha4 that correlate with repositioning of surrounding residues, like the active-site events indicator Trp54, putatively redifining the interaction with the ED in the full-length protein.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17182055}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17182055 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17182055}}
==About this Structure==
==About this Structure==
Line 47: Line 51:
[[Category: Transport]]
[[Category: Transport]]
[[Category: Two-component regulatory system]]
[[Category: Two-component regulatory system]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 08:38:34 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 19:15:39 2008''

Revision as of 16:15, 28 July 2008

Image:2jba.png

Template:STRUCTURE 2jba

PHOB RESPONSE REGULATOR RECEIVER DOMAIN CONSTITUTIVELY-ACTIVE DOUBLE MUTANT D53A AND Y102C.

Template:ABSTRACT PUBMED 17182055

About this Structure

2JBA is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

The X-ray crystal structures of two constitutively active mutants of the Escherichia coli PhoB receiver domain give insights into activation., Arribas-Bosacoma R, Kim SK, Ferrer-Orta C, Blanco AG, Pereira PJ, Gomis-Ruth FX, Wanner BL, Coll M, Sola M, J Mol Biol. 2007 Feb 16;366(2):626-41. Epub 2006 Nov 14. PMID:17182055

Page seeded by OCA on Mon Jul 28 19:15:39 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2jba"
Personal tools