Journal:Acta Cryst D:S2059798321009633
From Proteopedia
(Difference between revisions)
| Line 8: | Line 8: | ||
So far (2021), several 3D structures of SorC EBDs have been determined. They belong to the so-called NagB-like family for their homology with glucosamine 6 phosphate deaminases from the NagB family, characterized by the central Rossman fold<ref name="Rezacova">PMID:18554327</ref>,<ref name="Skerlova">PMID:24863636</ref>,<ref name="Sanctis">PMID:19232357</ref>. On the other hand, information on the structure of DNA-binding domains of SorC-family proteins is rather limited. SorC DBDs belong to the most abundant helix turn helix (HTH) superfamily and, by their sequences and structures, they cluster into two subfamilies: SorC/DeoR and SorC/CggR. | So far (2021), several 3D structures of SorC EBDs have been determined. They belong to the so-called NagB-like family for their homology with glucosamine 6 phosphate deaminases from the NagB family, characterized by the central Rossman fold<ref name="Rezacova">PMID:18554327</ref>,<ref name="Skerlova">PMID:24863636</ref>,<ref name="Sanctis">PMID:19232357</ref>. On the other hand, information on the structure of DNA-binding domains of SorC-family proteins is rather limited. SorC DBDs belong to the most abundant helix turn helix (HTH) superfamily and, by their sequences and structures, they cluster into two subfamilies: SorC/DeoR and SorC/CggR. | ||
| - | SorC/DeoR DBD is smaller and consists of the HTH bundle followed by a "β linker"<ref name="Sanctis">PMID:19232357</ref>, and the bigger SorC/CggR belong to the winged HTH family | + | SorC/DeoR DBD is smaller and consists of the HTH bundle followed by a "β linker"<ref name="Sanctis">PMID:19232357</ref>, and the bigger SorC/CggR belong to the winged HTH family<ref name="Doan">PMID:12622823</ref>. |
In this paper, we present the first structure of SorC DBDs bound to DNA duplexes. We show DBD structures of representatives of each subfamily, DeoR and CggR, and compare their binding mode, which is likely common to all SorC family members. | In this paper, we present the first structure of SorC DBDs bound to DNA duplexes. We show DBD structures of representatives of each subfamily, DeoR and CggR, and compare their binding mode, which is likely common to all SorC family members. | ||
| - | |||
| - | |||
| - | 8. Skerlova, J., Fabry, M., Hubalek, M., Otwinowski, Z. and Rezacova, P. (2014) Structure of the effectorâ€binding domain of deoxyribonucleoside regulator DeoR from Bacillus subtilis. The FEBS Journal, 281, 4280-4292. | ||
| - | 9. de Sanctis, D., McVey, C.E., Enguita, F.J. and Carrondo, M.A. (2009) Crystal structure of the full-length sorbitol operon regulator SorC from Klebsiella pneumoniae: structural evidence for a novel transcriptional regulation mechanism. J Mol Biol, 387, 759-770. | ||
| - | 10. Doan, T. and Aymerich, S. (2003) Regulation of the central glycolytic genes in Bacillus subtilis: binding of the repressor CggR to its single DNA target sequence is modulated by fructose-1,6-bisphosphate. Mol Microbiol, 47, 1709-1721. | ||
<b>References</b><br> | <b>References</b><br> | ||
Revision as of 12:22, 24 October 2021
| |||||||||||
This page complements a publication in scientific journals and is one of the Proteopedia's Interactive 3D Complement pages. For aditional details please see I3DC.
