Journal:Acta Cryst D:S2059798321009633
From Proteopedia
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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>,<ref name="Zeng">PMID:10714997</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>,<ref name="Zeng">PMID:10714997</ref>. | ||
| - | 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> | + | 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" | + | 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 (10). |
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. | ||
Revision as of 12:20, 24 October 2021
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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.
