LIS - Legume Information System
Information about legume traits for crop improvement
CicerMine
v5.1.0.3
Cicer data from the Legume Information System
v5.1.0.3
Cicer data from the Legume Information System
| Type | Conserved_site |
| Description | The many bacterial transcription regulation proteins which bind DNA through a 'helix-turn-helix' motif can be classified into subfamilies on the basis ofsequence similarities. One such family is the AsnC/Lrp subfamily [ ]. The Lrp family of transcriptional regulators appears to be widely distributed among bacteria andarchaea, as an important regulatory system of the amino acid metabolism and related processes [ ]. Members of the Lrp family are small DNA-binding proteins with molecular masses of around 15kDa. Target promoters often contain anumber of binding sites that typically lack obvious inverted repeat elements, and to which binding isusually co-operative. LrpA from Pyrococcus furiosus is the first Lrp-like protein to date of which a three-dimensional structure has been solved. In the crystal structure LrpA forms an octamer consistingof four dimers. The structure revealed that the N-terminal part of the protein consists of a helix-turn-helix (HTH) domain, a fold generally involved in DNA binding.The C terminus of Lrp-like proteins has a β-fold, where the two α-helices are located at one side of the four-stranded antiparallel β-sheet. LrpA forms a homodimer mainly through interactions between the β-strands of this C-terminaldomain, and an octamer through further interactions between the second α-helix and fourth β-strand of the motif. Hence, the C-terminal domain of Lrp-like proteins appears tobe involved in ligand-response and activation [ ].This entry represents a conserved site that spans the complete helix-turn-helix motif and extends one residue downstream and one upstream of the HTH extremities. |
| Short Name | Tscrpt_reg_HTH_AsnC-type_CS |
