2JZV
Solution structure of S. aureus PrsA-PPIase
Summary for 2JZV
| Entry DOI | 10.2210/pdb2jzv/pdb |
| Descriptor | Foldase protein prsA (1 entity in total) |
| Functional Keywords | ppiase, parvulin, foldase, staphylococcus aureus, proline isomerase, lipoprotein, membrane, palmitate, rotamase, isomerase |
| Biological source | Staphylococcus aureus |
| Cellular location | Cell membrane; Lipid-anchor (Potential): P60747 |
| Total number of polymer chains | 1 |
| Total formula weight | 12215.92 |
| Authors | Seppala, R.,Tossavainen, H.,Heikkinen, S.,Koskela, H.,Kontinen, V.,Permi, P. (deposition date: 2008-01-21, release date: 2009-01-20, Last modification date: 2024-05-29) |
| Primary citation | Heikkinen, O.,Seppala, R.,Tossavainen, H.,Heikkinen, S.,Koskela, H.,Permi, P.,Kilpelainen, I. Solution structure of the parvulin-type PPIase domain of Staphylococcus aureus PrsA - Implications for the catalytic mechanism of parvulins. Bmc Struct.Biol., 9:17-17, 2009 Cited by PubMed Abstract: Staphylococcus aureus is a Gram-positive pathogenic bacterium causing many kinds of infections from mild respiratory tract infections to life-threatening states as sepsis. Recent emergence of S. aureus strains resistant to numerous antibiotics has created a need for new antimicrobial agents and novel drug targets. S. aureus PrsA is a membrane associated extra-cytoplasmic lipoprotein which contains a parvulin-type peptidyl-prolyl cis-trans isomerase domain. PrsA is known to act as an essential folding factor for secreted proteins in Gram-positive bacteria and thus it is a potential target for antimicrobial drugs against S. aureus. PubMed: 19309529DOI: 10.1186/1472-6807-9-17 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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