1ZK6
NMR solution structure of B. subtilis PrsA PPIase
Summary for 1ZK6
| Entry DOI | 10.2210/pdb1zk6/pdb |
| Descriptor | Foldase protein prsA (1 entity in total) |
| Functional Keywords | alpha/beta structure, isomerase |
| Biological source | Bacillus subtilis |
| Cellular location | Cell membrane; Lipid-anchor (Potential): P24327 |
| Total number of polymer chains | 1 |
| Total formula weight | 10307.61 |
| Authors | Tossavainen, H.,Permi, P.,Purhonen, S.L.,Sarvas, M.,Kilpelainen, I.,Seppala, R. (deposition date: 2005-05-02, release date: 2006-03-28, Last modification date: 2024-05-22) |
| Primary citation | Tossavainen, H.,Permi, P.,Purhonen, S.L.,Sarvas, M.,Kilpelainen, I.,Seppala, R. NMR solution structure and characterization of substrate binding site of the PPIase domain of PrsA protein from Bacillus subtilis Febs Lett., 580:1822-1826, 2006 Cited by PubMed Abstract: PrsA is a peptidyl-prolyl isomerase (PPIase) from Bacillus subtilis belonging to the parvulin family of PPIases. It is a membrane bound lipoprotein at the membrane-wall interface, involved in folding of exported proteins. We present the NMR solution structure of the PPIase domain of PrsA, the first from a Gram-positive bacterium. In addition we mapped out the active site with NMR titration experiments. A high degree of conservation with other members of the parvulin family was revealed in the structure and binding site. Interactions with substrate peptides were also characterized by mutated domains revealing that H122 is indispensable for overall correct folding. PubMed: 16516208DOI: 10.1016/j.febslet.2006.02.042 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
