2ek5: Difference between revisions
New page: left|200px<br /><applet load="2ek5" size="350" color="white" frame="true" align="right" spinBox="true" caption="2ek5, resolution 2.2Å" /> '''Crystal strucutre of ... |
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==Overview== | ==Overview== | ||
Among the transcription factors, the helix-turn-helix (HTH) GntR family | 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. | ||
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
The structures of transcription factor CGL2947 from Corynebacterium glutamicum in two crystal forms: | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17766384 17766384] | ||
[[Category: Corynebacterium glutamicum]] | [[Category: Corynebacterium glutamicum]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Gao, Y | [[Category: Gao, Y G.]] | ||
[[Category: Tanaka, I.]] | [[Category: Tanaka, I.]] | ||
[[Category: Yao, M.]] | [[Category: Yao, M.]] | ||
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[[Category: transcription]] | [[Category: transcription]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:11:40 2008'' | ||
Revision as of 18:11, 21 February 2008
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Crystal strucutre of the transcriptional factor from C.glutamicum at 2.2 angstrom resolution
OverviewOverview
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.
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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