5W95
Mtb Rv3802c with PEG bound
Summary for 5W95
| Entry DOI | 10.2210/pdb5w95/pdb |
| Descriptor | Conserved membrane protein of uncharacterised function, PENTAETHYLENE GLYCOL (3 entities in total) |
| Functional Keywords | peg, complex, hydrolase |
| Biological source | Mycobacterium tuberculosis |
| Total number of polymer chains | 2 |
| Total formula weight | 61552.82 |
| Authors | Goins, C.M.,Schreidah, C.M.,Ronning, D.R. (deposition date: 2017-06-22, release date: 2017-12-27, Last modification date: 2024-11-06) |
| Primary citation | Goins, C.M.,Schreidah, C.M.,Dajnowicz, S.,Ronning, D.R. Structural basis for lipid binding and mechanism of the Mycobacterium tuberculosis Rv3802 phospholipase. J. Biol. Chem., 293:1363-1372, 2018 Cited by PubMed Abstract: The gene encodes an essential enzyme with thioesterase and phospholipase A activity. Overexpression of Rv3802 orthologs in and increases mycolate content and decreases glycerophospholipids. Although a role in modulating the lipid composition of the unique mycomembrane has been proposed, the true biological function of Rv3802 remains uncertain. In this study, we present the first Rv3802 X-ray crystal structure, solved to 1.7 Å resolution. On the basis of the binding of PEG molecules to Rv3802, we identified its lipid-binding site and the structural basis for phosphatidyl-based substrate binding and phospholipase A activity. We found that movement of the α8-helix affords lipid binding and is required for catalytic turnover through covalent tethering. We gained insights into the mechanism of acyl hydrolysis by observing differing arrangements of PEG and water molecules within the active site. This study provides structural insights into biological function and facilitates future structure-based drug design toward Rv3802. PubMed: 29247008DOI: 10.1074/jbc.RA117.000240 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.723 Å) |
Structure validation
Download full validation report
