Journal:Acta Cryst D:S2059798322001772
From Proteopedia
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The LmcA structure revealed an elongated beta-barrel fold and one alpha-helix extending away from the beta-barrel core. Interestingly, two distinct cavities were found inside the protein which could bind a ligand. Further analysis revealed elements in LmcA that may undergo conformational changes to ‘open’ the protein, permitting access to the cavities. While the ligand remains to be identified, comparison of the crystal structure with LmcA models from other bacterial species suggests a common mechanism of ligand binding involving the cavities. These findings provide new structural insights into the biosynthetic pathway for PIM/LM/LAM, essential components of the mycobacterial cell surface. | The LmcA structure revealed an elongated beta-barrel fold and one alpha-helix extending away from the beta-barrel core. Interestingly, two distinct cavities were found inside the protein which could bind a ligand. Further analysis revealed elements in LmcA that may undergo conformational changes to ‘open’ the protein, permitting access to the cavities. While the ligand remains to be identified, comparison of the crystal structure with LmcA models from other bacterial species suggests a common mechanism of ligand binding involving the cavities. These findings provide new structural insights into the biosynthetic pathway for PIM/LM/LAM, essential components of the mycobacterial cell surface. | ||
| - | <scene name='90/906221/Cv/ | + | <scene name='90/906221/Cv/4'>The crystal structure of MSMEG_0317</scene> adopts an extended beta-barrel core composed of 11 antiparallel beta-strands with two alpha-turns and one alpha-helix extending away from the core. The secondary structure elements are shown in distinct colours. |
<b>References</b><br> | <b>References</b><br> | ||
Revision as of 10:30, 7 March 2022
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