1ysf
From Proteopedia
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- | [[Image:1ysf.jpg|left|200px]] | + | [[Image:1ysf.jpg|left|200px]] |
- | + | ||
- | '''The solution structure of the N-domain of the transcription factor abrB''' | + | {{Structure |
+ | |PDB= 1ysf |SIZE=350|CAPTION= <scene name='initialview01'>1ysf</scene> | ||
+ | |SITE= | ||
+ | |LIGAND= | ||
+ | |ACTIVITY= | ||
+ | |GENE= ABRB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis]) | ||
+ | }} | ||
+ | |||
+ | '''The solution structure of the N-domain of the transcription factor abrB''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1YSF is a [ | + | 1YSF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YSF OCA]. |
==Reference== | ==Reference== | ||
- | AbrB-like transcription factors assume a swapped hairpin fold that is evolutionarily related to double-psi beta barrels., Coles M, Djuranovic S, Soding J, Frickey T, Koretke K, Truffault V, Martin J, Lupas AN, Structure. 2005 Jun;13(6):919-28. PMID:[http:// | + | AbrB-like transcription factors assume a swapped hairpin fold that is evolutionarily related to double-psi beta barrels., Coles M, Djuranovic S, Soding J, Frickey T, Koretke K, Truffault V, Martin J, Lupas AN, Structure. 2005 Jun;13(6):919-28. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15939023 15939023] |
[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: nmr; homodimer; bioinformatics; swapped-hairpin barrel]] | [[Category: nmr; homodimer; bioinformatics; swapped-hairpin barrel]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:26:56 2008'' |
Revision as of 13:27, 20 March 2008
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Gene: | ABRB (Bacillus subtilis) | ||||||
Coordinates: | save as pdb, mmCIF, xml |
The solution structure of the N-domain of the transcription factor abrB
Overview
AbrB is a key transition-state regulator of Bacillus subtilis. Based on the conservation of a betaalphabeta structural unit, we proposed a beta barrel fold for its DNA binding domain, similar to, but topologically distinct from, double-psi beta barrels. However, the NMR structure revealed a novel fold, the "looped-hinge helix." To understand this discrepancy, we undertook a bioinformatics study of AbrB and its homologs; these form a large superfamily, which includes SpoVT, PrlF, MraZ, addiction module antidotes (PemI, MazE), plasmid maintenance proteins (VagC, VapB), and archaeal PhoU homologs. MazE and MraZ form swapped-hairpin beta barrels. We therefore reexamined the fold of AbrB by NMR spectroscopy and found that it also forms a swapped-hairpin barrel. The conservation of the core betaalphabeta element supports a common evolutionary origin for swapped-hairpin and double-psi barrels, which we group into a higher-order class, the cradle-loop barrels, based on the peculiar shape of their ligand binding site.
About this Structure
1YSF is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
AbrB-like transcription factors assume a swapped hairpin fold that is evolutionarily related to double-psi beta barrels., Coles M, Djuranovic S, Soding J, Frickey T, Koretke K, Truffault V, Martin J, Lupas AN, Structure. 2005 Jun;13(6):919-28. PMID:15939023
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