3V1H
Structure of the H258Y mutant of Phosphatidylinositol-specific phospholipase C from Staphylococcus aureus
Summary for 3V1H
| Entry DOI | 10.2210/pdb3v1h/pdb |
| Related | 3v16 3v18 |
| Descriptor | 1-phosphatidylinositol phosphodiesterase, 1,2,3,4,5,6-HEXAHYDROXY-CYCLOHEXANE, ACETATE ION, ... (4 entities in total) |
| Functional Keywords | pi-cation, tim barrel, phospholipase, lyase |
| Biological source | Staphylococcus aureus subsp. aureus |
| Total number of polymer chains | 1 |
| Total formula weight | 35086.96 |
| Authors | Goldstein, R.I.,Cheng, J.,Stec, B.,Roberts, M.F. (deposition date: 2011-12-09, release date: 2012-04-04, Last modification date: 2023-09-13) |
| Primary citation | Goldstein, R.,Cheng, J.,Stec, B.,Roberts, M.F. Structure of the S. aureus PI-Specific Phospholipase C Reveals Modulation of Active Site Access by a Titratable PI-Cation Latched Loop Biochemistry, 51:2579-2587, 2012 Cited by PubMed Abstract: Staphylococcus aureus secretes a phosphatidylinositol-specific phospholipase C (PI-PLC) as a virulence factor that is unusual in exhibiting higher activity at acidic pH values than other enzymes in this class. We have determined the crystal structure of this enzyme at pH 4.6 and pH 7.5. Under slightly basic conditions, the S. aureus PI-PLC structure closely follows the conformation of other bacterial PI-PLCs. However, when crystallized under acidic conditions, a large section of mobile loop at the αβ-barrel rim in the vicinity of the active site shows ~10 Å shift. This loop displacement at acidic pH is the result of a titratable intramolecular π-cation interaction between His258 and Phe249. This was verified by a structure of the mutant protein H258Y crystallized at pH 4.6, which does not exhibit the large loop shift. The intramolecular π-cation interaction for S. aureus PI-PLC provides an explanation for the activity of the enzyme at acid pH and also suggests how phosphatidylcholine, as a competitor for Phe249, may kinetically activate this enzyme. PubMed: 22390775DOI: 10.1021/bi300057q PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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