1ysf: Difference between revisions
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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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| 1ysf | |||||||||||||
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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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