LIS - Legume Information System
Information about legume traits for crop improvement
GlycineMine
v5.1.0.3
Glycine data from LIS
v5.1.0.3
Glycine data from LIS
| Type | Domain |
| Description | This domain is found at the C-terminal of bacterial regulatory ATPase RavA (Regulatory ATPase variant A) [ , ]. RavA consists of three domains: the N-terminal domain is the AAA+ module, which is composed of two subdomains, the α-β-alpha subdomain with a Rossmann-type fold commonly found in nucleotide binding proteins and the all-alpha subdomain consisting of four antiparallel α-helices; the second domain is a discontinuous triple-helical domain which has a rigid structure stabilised by hydrophobic interactions localised at the interface between the three helices; and the third domain, named the LARA domain which forms a compact antiparallel β-barrel-like structure consisting of six β-strands and one α-helix [, ]. RavA forms an hexamer in which the triple helical domain mediates the lateral interactions between neighbouring RavA monomers []. This is the second subdomain that forms the discontinuous triple helical domain [ ] and contains single completely conserved phenylalanine residue that makes hydrophobic contacts with the AAA+ module resulting in anchoring the triple-helical domain to the AAA+ module. This conserved Phe might serve to transmit the nucleotide-dependent conformational changes in the AAA+ domain to the C-terminal triple-helical and LARA domains of RavA []. |
| Short Name | ATPase_RavA_C |
