Journal:Acta Cryst F:S2053230X18016217
From Proteopedia
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<b>Molecular Tour</b><br> | <b>Molecular Tour</b><br> | ||
| - | There are three HtrA paralogues in ''M. tuberculosis'' viz., HtrA (Rv1223), PepD (Rv0983) and PepA (Rv0125). Among these, only HtrA is essential for bacterial survival. ''M. tuberculosis'' PepD participates in a two component signaling pathway involving MprAB and | + | There are three HtrA paralogues in ''M. tuberculosis'' viz., HtrA (Rv1223), PepD (Rv0983) and PepA (Rv0125). Among these, only HtrA is essential for bacterial survival. ''M. tuberculosis'' PepD participates in a two component signaling pathway involving MprAB and σ<sup>E</sup>. It has been suggested that recognition of misfolded proteins by the PDZ domain in PepD activates this pathway. However, unlike DegS, this HtrA homologue is constitutively active and the PDZ domain positively modulates its enzymatic activity. An aspect that is less explored in this context is the role of the N-terminal cytoplasmic domain. Both HtrA and PepD are predicted to have a cytoplasmic polypeptide stretch of 100-150 residues. |
A common structural feature of HtrA proteases is that of a trypsin-like serine protease domain attached to one or more PDZ domains. An ''in silico'' analysis of the topological arrangement of these proteases suggests that they are likely to adopt a similar Nin-Cout conformation with one transmembrane helix. Given substantial sequence and structural conservation, the precise roles as well as the rationale for multiple HtrA paralogues in a bacterium are difficult to predict. This aspect is of particular significance to ''M. tuberculosis'' as HtrA enzymes govern virulence but the molecular details remain unclear. | A common structural feature of HtrA proteases is that of a trypsin-like serine protease domain attached to one or more PDZ domains. An ''in silico'' analysis of the topological arrangement of these proteases suggests that they are likely to adopt a similar Nin-Cout conformation with one transmembrane helix. Given substantial sequence and structural conservation, the precise roles as well as the rationale for multiple HtrA paralogues in a bacterium are difficult to predict. This aspect is of particular significance to ''M. tuberculosis'' as HtrA enzymes govern virulence but the molecular details remain unclear. | ||
Revision as of 07:02, 26 November 2018
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