2fyi

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2fyi.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2fyi.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2fyi| PDB=2fyi | SCENE= }}
{{STRUCTURE_2fyi| PDB=2fyi | SCENE= }}
-
'''Crystal Structure of the Cofactor-Binding Domain of the Cbl Transcriptional Regulator'''
+
===Crystal Structure of the Cofactor-Binding Domain of the Cbl Transcriptional Regulator===
-
==Overview==
+
<!--
-
Cbl is a member of the large family of LysR-type transcriptional regulators (LTTRs) common in bacteria and found also in Archaea and algal chloroplasts. The function of Cbl is required in Escherichia coli for expression of sulphate starvation-inducible (ssi) genes, associated with the biosynthesis of cysteine from organic sulphur sources (sulphonates). Here, we report the crystal structure of the cofactor-binding domain of Cbl (c-Cbl) from E. coli. The overall fold of c-Cbl is very similar to the regulatory domain (RD) of another LysR family member, CysB. The RD is composed of two subdomains enclosing a cavity, which is expected to bind effector molecules. We have constructed and analysed several full-length Cbl variants bearing single residue substitutions in the RD that affect cofactor responses. Using in vivo and in vitro transcription assays, we demonstrate that pssuE, a Cbl responsive promoter, is down-regulated not only by the cofactor, adenosine phosphosulphate (APS), but also by thiosulphate, and, that the same RD determinants are important for the response to both cofactors. We also demonstrate the effects of selected site-directed mutations on Cbl oligomerization and discuss these in the context of the structure. Based on the crystal structure and molecular modelling, we propose a model for the interaction of Cbl with adenosine phosphosulphate.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17010379}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17010379 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17010379}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Lys-r family]]
[[Category: Lys-r family]]
[[Category: Transcriptional regulator]]
[[Category: Transcriptional regulator]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 04:27:08 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 16:13:23 2008''

Revision as of 13:13, 29 July 2008

Image:2fyi.png

Template:STRUCTURE 2fyi

Crystal Structure of the Cofactor-Binding Domain of the Cbl Transcriptional Regulator

Template:ABSTRACT PUBMED 17010379

About this Structure

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

Reference

Structural basis of the sulphate starvation response in E. coli: crystal structure and mutational analysis of the cofactor-binding domain of the Cbl transcriptional regulator., Stec E, Witkowska-Zimny M, Hryniewicz MM, Neumann P, Wilkinson AJ, Brzozowski AM, Verma CS, Zaim J, Wysocki S, Bujacz GD, J Mol Biol. 2006 Dec 1;364(3):309-22. Epub 2006 Jun 30. PMID:17010379

Page seeded by OCA on Tue Jul 29 16:13:23 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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