3B18
Rv0098 of Mycobacterium tuberculosis with ordered loop between beta-4 and beta-5
Summary for 3B18
| Entry DOI | 10.2210/pdb3b18/pdb |
| Related | 2PFC |
| Descriptor | Uncharacterized protein Rv0098/MT0107, LAURIC ACID (3 entities in total) |
| Functional Keywords | hot dog fold, long-chain fatty acyl-coa thioesterase, acyl carrier protein, mycobacterium tuberculosis, hydrolase |
| Biological source | Mycobacterium tuberculosis |
| Total number of polymer chains | 1 |
| Total formula weight | 20749.80 |
| Authors | Maity, K.,Suguna, K. (deposition date: 2011-06-26, release date: 2012-06-06, Last modification date: 2024-10-30) |
| Primary citation | Maity, K.,Bajaj, P.,Surolia, N.,Surolia, A.,Suguna, K. Insights into the substrate specificity of a thioesterase Rv0098 of mycobacterium tuberculosis through X-ray crystallographic and molecular dynamics studies. J.Biomol.Struct.Dyn., 29:973-983, 2012 Cited by PubMed Abstract: The crystal structure of Rv0098, a long-chain fatty acyl-CoA thioesterase from Mycobacterium tuberculosis with bound dodecanoic acid at the active site provided insights into the mode of substrate binding but did not reveal the structural basis of substrate specificities of varying chain length. Molecular dynamics studies demonstrated that certain residues of the substrate binding tunnel are flexible and thus modulate the length of the tunnel. The flexibility of the loop at the base of the tunnel was also found to be important for determining the length of the tunnel for accommodating appropriate substrates. A combination of crystallographic and molecular dynamics studies thus explained the structural basis of accommodating long chain substrates by Rv0098 of M. tuberculosis. PubMed: 22292955DOI: 10.1080/07391102.2012.10507417 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.75 Å) |
Structure validation
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