Journal:Acta Cryst D:S2059798321009633
From Proteopedia
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<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> (2-4) or LsrR (5,6). 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 (4,7). | + | 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> (2-4) or LsrR (5,6). 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 (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. |
SorC/DeoR DBD is smaller and consists of the HTH bundle followed by a "β linker" (9), and the bigger SorC/CggR belong to the winged HTH family (10). | SorC/DeoR DBD is smaller and consists of the HTH bundle followed by a "β linker" (9), and the bigger SorC/CggR belong to the winged HTH family (10). | ||
Revision as of 10:17, 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.
