Journal:Acta Cryst D:S2059798321009633
From Proteopedia
(Difference between revisions)
| Line 5: | Line 5: | ||
<hr/> | <hr/> | ||
<b>Molecular Tour</b><br> | <b>Molecular Tour</b><br> | ||
| - | SorC (SorC/DeoR) protein family (Pfam family Sugar-bind: PF04198<ref name="Finn">PMID:18039703</ref>) is one of the large families of bacterial transcriptional regulators, predominantly repressors, that are known for their roles in the regulation of carbohydrate metabolism and quorum-sensing in more than 2,500 bacterial species. For example, among the most studied members are CggR<ref name="Chaix">PMID:20462860</ref>,<ref name="Rezacova">PMID:18554327</ref>,<ref name="Zorilla">PMID:17293407</ref> | + | SorC (SorC/DeoR) protein family (Pfam family Sugar-bind: PF04198<ref name="Finn">PMID:18039703</ref>) is one of the large families of bacterial transcriptional regulators, predominantly repressors, that are known for their roles in the regulation of carbohydrate metabolism and quorum-sensing in more than 2,500 bacterial species. For example, among the most studied members are CggR<ref name="Chaix">PMID:20462860</ref>,<ref name="Rezacova">PMID:18554327</ref>,<ref name="Zorilla">PMID:17293407</ref> or LsrR<ref name="Xavier">PMID:15601708</ref>,<ref name="Ha">PMID:24047255</ref>. SorC protomers consist of a large C terminal effector binding domain (EBD) and a much smaller N terminal DNA binding domain (DBD). As an assembly, SorC proteins work as tetramers in a cooperative manner, to our best knowledge<ref name="Zorilla">PMID:17293407</ref> (4,7). |
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> (3,8,9). 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> (3,8,9). 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. | ||
| Line 14: | Line 14: | ||
References: | References: | ||
| - | 2. Chaix, D., Ferguson, M.L., Atmanene, C., Dorsselaer, A.V., Sanglier-Cianférani, S., Royer, C.A. and Declerck, N. (2010) Physical basis of the inducer-dependent cooperativity of the Central glycolytic genes Repressor/DNA complex. Nucleic Acids Res, 38, 5944-5957. | ||
| - | 3. Rezacova, P., Kozisek, M., Moy, S.F., Sieglova, I., Joachimiak, A., Machius, M. and Otwinowski, Z. (2008) Crystal structures of the effector-binding domain of repressor Central glycolytic gene Regulator from Bacillus subtilis reveal ligand-induced structural changes upon binding of several glycolytic intermediates. Molecular Microbiology, 69, 895-910. | ||
| - | 4. Zorilla, S., Doan, T., Alfonso, C., Margeat, E., Ortega, A., Rivas, G., Aymerich, S., Royer, C.A. and Declerck, N. (2007) Inducer-Modulated Cooperative Binding of the Tetrameric CggR Repressor to Operator DNA. Biohysical Journal, 92, 3215-3227. | ||
| - | 5. Xavier, K.B. and Bassler, B.L. (2005) Regulation of uptake and processing of the quorum-sensing autoinducer AI-2 in Escherichia coli. J Bacteriol, 187, 238-248. | ||
| - | 6. Ha, J.H., Eo, Y., Grishaev, A., Guo, M., Smith, J.A., Sintim, H.O., Kim, E.H., Cheong, H.K., Bentley, W.E. and Ryu, K.S. (2013) Crystal structures of the LsrR proteins complexed with phospho-AI-2 and two signal-interrupting analogues reveal distinct mechanisms for ligand recognition. J Am Chem Soc, 135, 15526-15535. | ||
7. Zeng, X., Saxild, H.H. and Switzer, R.L. (2000) Purification and Characterization of the DeoR Repressor of Bacillus subtilis. Journal of Bacteriology, 182, 1916-1922. | 7. Zeng, X., Saxild, H.H. and Switzer, R.L. (2000) Purification and Characterization of the DeoR Repressor of Bacillus subtilis. Journal of Bacteriology, 182, 1916-1922. | ||
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. | 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. | ||
Revision as of 10:22, 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.
