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2aje
From Proteopedia
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[[Image:2aje.gif|left|200px]] | [[Image:2aje.gif|left|200px]] | ||
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'''Solution structure of the Arabidopsis thaliana telomeric repeat-binding protein DNA binding domain''' | '''Solution structure of the Arabidopsis thaliana telomeric repeat-binding protein DNA binding domain''' | ||
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[[Category: Huang, T H.]] | [[Category: Huang, T H.]] | ||
[[Category: Sue, S C.]] | [[Category: Sue, S C.]] | ||
| - | [[Category: | + | [[Category: Dna-binding]] |
| - | [[Category: | + | [[Category: Myb motif]] |
| - | [[Category: | + | [[Category: Telomere]] |
| - | [[Category: | + | [[Category: Trp]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:07:27 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 16:07, 3 May 2008
Solution structure of the Arabidopsis thaliana telomeric repeat-binding protein DNA binding domain
Overview
The double-stranded telomeric repeat-binding protein (TRP) AtTRP1 is isolated from Arabidopsis thaliana. Using gel retardation assays, we defined the C-terminal 97 amino acid residues, Gln464 to Val560 (AtTRP1(464-560)), as the minimal structured telomeric repeat-binding domain. This region contains a typical Myb DNA-binding motif and a C-terminal extension of 40 amino acid residues. The monomeric AtTRP1(464-560) binds to a 13-mer DNA duplex containing a single repeat of an A.thaliana telomeric DNA sequence (GGTTTAG) in a 1:1 complex, with a K(D) approximately 10(-6)-10(-7) M. Nuclear magnetic resonance (NMR) examination revealed that the solution structure of AtTRP1(464-560) is a novel four-helix tetrahedron rather than the three-helix bundle structure found in typical Myb motifs and other TRPs. Binding of the 13-mer DNA duplex to AtTRP1(464-560) induced significant chemical shift perturbations of protein amide resonances, which suggests that helix 3 (H3) and the flexible loop connecting H3 and H4 are essential for telomeric DNA sequence recognition. Furthermore, similar to that in hTRF1, the N-terminal arm likely contributes to or stabilizes DNA binding. Sequence comparisons suggested that the four-helix structure and the involvement of the loop residues in DNA binding may be features unique to plant TRPs.
About this Structure
2AJE is a Single protein structure of sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA.
Reference
Solution structure of the Arabidopsis thaliana telomeric repeat-binding protein DNA binding domain: a new fold with an additional C-terminal helix., Sue SC, Hsiao HH, Chung BC, Cheng YH, Hsueh KL, Chen CM, Ho CH, Huang TH, J Mol Biol. 2006 Feb 10;356(1):72-85. Epub 2005 Nov 22. PMID:16337232 Page seeded by OCA on Sat May 3 19:07:27 2008
Categories: Arabidopsis thaliana | Single protein | Cheng, Y H. | Chung, B C. | Hsiao, H H. | Huang, T H. | Sue, S C. | Dna-binding | Myb motif | Telomere | Trp
