AF-Sm1: Difference between revisions

'''AF-Sm1''', found the in the bacteria Archaeoglobus fulgidus is a member of a family called Sm and Sm-like (Lsm) proteins. This protein forms a heptameric structure and contains 1 α-helix, 5 β-sheets, and 5 loops between the α-helix and each of the β-sheets. Contained in the protein are two <scene name='Sandbox_175/Ligand_view/1'>ligands</scene>. The structure contains a predominate fold, called the Sm-fold which consists of an N-terminal helix followed by a sharply bent five-stranded β-sheet which leads to the protein having a barrel-type structure, commonly referred to as a “doughnut-shape.”<ref name="AFSM1">PMID:11331594</ref> Uninterrupted hydrogen bonding occurs between β-sheets 4 and 5, leading to residues in loops 2, 3, and 5 being exposed at the inner surface of the ring and both the N and C termini being located at the outer surface of the ring.<ref name="AFSM1"/> A lysine residue located on loop 2 protrudes into the central cavity of the protein creating a positively charged region surrounding the central cavity on one side of the rings. <ref name="AFSM1"/> This protein has been linked due to its close structural resemblance, including sharing the Sm-fold structure, to the human dimeric D3/B and D1/D2 Sm complexes.<ref name="AFSM1"/>.  See [[Transcription and RNA Processing]].