2ek5: Difference between revisions

Revision as of 10:59, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2ek5.png

Template:STRUCTURE 2ek5

Crystal strucutre of the transcriptional factor from C.glutamicum at 2.2 angstrom resolutionCrystal strucutre of the transcriptional factor from C.glutamicum at 2.2 angstrom resolution

Template:ABSTRACT PUBMED 17766384

About this StructureAbout this Structure

2EK5 is a Single protein structure of sequence from Corynebacterium glutamicum. Full crystallographic information is available from OCA.

ReferenceReference

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

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-'''Crystal strucutre of the transcriptional factor from C.glutamicum at 2.2 angstrom resolution'''
+===Crystal strucutre of the transcriptional factor from C.glutamicum at 2.2 angstrom resolution===
-==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.
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+{{ABSTRACT_PUBMED_17766384}}
 ==About this Structure==
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 [[Category: Interwined alpha helice]]
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