| Primary Identifier | IPR029220 | Type | Homologous_superfamily |
| Short Name | BP-Tp47_dom_D |
| description | The crystal structure of the unusual penicillin-binding protein (PBP) Tp47 from Treponema pallidum revealed a unique structure different to any other known PBP, and thus it appears to represent an entirely new class of PBP. Tp47 consists of four distinct domains (A-D) arranged to give the molecule a crab-like appearance. Domain D, like domain C, features an immunoglobulin fold. In contrast to domain C it contains only the characteristic seven-stranded barrel and short loops. As in domain C, a single α-helical turn is inserted between strands 2 and 3 []. Domain D is rather isolated as it only interacts with domain C via an ionic interaction between Arg-330 and Glu-404 in the linker region. This explains the large degree of motion observed for this domain.The abundance of hydrophobic residues and the immunoglobulin fold of domain D suggests that it mediates protein-protein interactions. In addition its location, flexibility, and relative disposition indicate a function other that PBP and beta-lactamase activities []. It is thought to have an haemagglutination activity. |
