We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

2du9

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2du9.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2du9.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2du9| PDB=2du9 | SCENE= }}
{{STRUCTURE_2du9| PDB=2du9 | SCENE= }}
-
'''crystal structure of the transcriptional factor from C.glutamicum'''
+
===crystal structure of the transcriptional factor from C.glutamicum===
-
==Overview==
+
<!--
-
Among the transcription factors, the helix-turn-helix (HTH) GntR family comprised of FadR, HutC, MocR, YtrA, AraR, and PlmA subfamilies regulates the most varied biological processes. Generally, proteins belonging to this family contain an N-terminal DNA-binding domain and a C-terminal effector-binding/oligomerization domain. The members of the YtrA subfamily are much shorter than other members of this family, with chain lengths of 120-130 residues with about 50 residues located in the C-terminal domain. Because of this length, the mode of dimerization and the ability to bind effectors by the C-terminal domain are puzzling. Here, we first report the structure of the transcription factor CGL2947 from Corynebacterium glutamicum, which belongs to the YtrA family. The monomer is composed of a DNA-binding domain containing a winged HTH motif in the N terminus and two helices (alpha4 and alpha5) with a fishhook-shaped arrangement in the C terminus. Helices alpha4 and alpha5 of two monomers intertwine together to form a novel homodimer assembly. The effector-accommodating pocket with 2-methyl-2,4-pentanediol (MPD) docked was located, and it was suggested to represent a novel mode of effector binding. The structures in two crystal forms (MPD-free and -bound in the proposed effector-binding pocket) were solved. The structural variations have implications regarding how the effector-induced conformational change modulates DNA affinity for YtrA family members.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17766384}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17766384 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17766384}}
==About this Structure==
==About this Structure==
Line 26: Line 30:
[[Category: Yao, M.]]
[[Category: Yao, M.]]
[[Category: Winged helix-turn-helix]]
[[Category: Winged helix-turn-helix]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 01:23:24 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 07:35:10 2008''

Revision as of 04:35, 28 July 2008

Image:2du9.png

Template:STRUCTURE 2du9

crystal structure of the transcriptional factor from C.glutamicum

Template:ABSTRACT PUBMED 17766384

About this Structure

2DU9 is a Single protein structure of sequence from Corynebacterium glutamicum. Full crystallographic information is available from OCA.

Reference

The structures of transcription factor CGL2947 from Corynebacterium glutamicum in two crystal forms: a novel homodimer assembling and the implication for effector-binding mode., Gao YG, Yao M, Itou H, Zhou Y, Tanaka I, Protein Sci. 2007 Sep;16(9):1878-86. PMID:17766384

Page seeded by OCA on Mon Jul 28 07:35:10 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2du9"
Personal tools