Journal:Acta Cryst F:S2053230X18016217
From Proteopedia
(Difference between revisions)
| Line 8: | Line 8: | ||
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. | ||
| - | The crystal structure of ''M. tuberculosis'' HtrA (ΔTM HtrA) that was determined at 1.83 Å resolution. We note that this enzyme exhibits both monomeric as well as trimeric forms in solution. The structure reveals a conformation that would require minor structural alterations for proteolytic activity. Structural features thus suggest that ''M. tuberculosis'' HtrA is a regulated protease as opposed to the two other paralogues, PepD and PepA. This essential enzyme is thus likely to be involved in specific signal transduction role as opposed to housekeeping in the recognition and degradation of partially folded or misfolded proteins. | + | The crystal structure of ''M. tuberculosis'' HtrA (ΔTM HtrA) that was determined at 1.83 Å resolution. We note that this enzyme exhibits both monomeric as well as trimeric forms in solution. The structure reveals a conformation that would require minor structural alterations for proteolytic activity. Structural features thus suggest that ''M. tuberculosis'' HtrA is a regulated protease as opposed to the two other paralogues, PepD and PepA. This essential enzyme is thus likely to be involved in specific signal transduction role as opposed to housekeeping in the recognition and degradation of partially folded or misfolded proteins. |
| - | + | ||
| + | The <scene name='80/801748/Cv/2'>crystal structure of ΔTM HtrA</scene> was determined at a resolution of 1.83Å (PDB ID: [[6ieo]]). In this crystal form, there is one molecule of HtrA in the asymmetric unit. | ||
<b>References</b><br> | <b>References</b><br> | ||
Revision as of 07:02, 26 November 2018
| |||||||||||
This page complements a publication in scientific journals and is one of the Proteopedia's Interactive 3D Complement pages. For aditional details please see I3DC.
