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 | Most Clp ATPases form complexes with peptidase subunits and are involved in protein degradation, though some, such as ClpB, do not associate with peptidases and are involved in protein disaggregation [ ]. This entry represents the C-terminal domain of Clp ATPases, often referred to as the D2-small domain, which forms a mixed α-β structure. Compared with the adjacent AAA D1-small domain () it lacks the long coiled-coil insertion, and instead of helix C4 contains a β-strand (e3) that is part of a three stranded β-pleated sheet. In Thermophilus the whole protein forms a hexamer with the D1-small and D2-small domains located on the outside of the hexamer, with the long coiled-coil being exposed on the surface. The D2-small domain is essential for oligomerisation, forming a tight interface with the D2-large domain of a neighbouring subunit, thereby providing enough binding energy to stabilise the functional assembly [ ]. |
| Short Name | Clp_ATPase_C |
