Journal:Acta Cryst F:S2053230X18016217
From Proteopedia
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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. The structure of the periplasmic domain reveals one <scene name='80/801748/Cv/3'>trypsin-like protease domain</scene> (<span style="color:royalblue;background-color:black;font-weight:bold;">226-436; colored in royalblue</span>) flexibly tethered to the <scene name='80/801748/Cv/4'>PDZ domain</scene> (443-528;) at the C-terminal end. | + | 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. The structure of the periplasmic domain reveals one <scene name='80/801748/Cv/3'>trypsin-like protease domain</scene> (<span style="color:royalblue;background-color:black;font-weight:bold;">226-436; colored in royalblue</span>) flexibly tethered to the <scene name='80/801748/Cv/4'>PDZ domain</scene> (<span style="color:gold;background-color:black;font-weight:bold;">443-528; in gold</span>) at the C-terminal end. |
<b>References</b><br> | <b>References</b><br> | ||
Revision as of 07:18, 26 November 2018
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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.
