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Recent emergence of <jats:italic>S. aureus<\/jats:italic> strains resistant to numerous antibiotics has created a need for new antimicrobial agents and novel drug targets. <jats:italic>S. aureus<\/jats:italic> PrsA is a membrane associated extra-cytoplasmic lipoprotein which contains a parvulin-type peptidyl-prolyl <jats:italic>cis-trans<\/jats:italic> 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 <jats:italic>S. aureus<\/jats:italic>.<\/jats:p>\n          <\/jats:sec>\n          <jats:sec>\n            <jats:title>Results<\/jats:title>\n            <jats:p>We have solved a high-resolution solution structure of the parvulin-type peptidyl-prolyl <jats:italic>cis-trans<\/jats:italic> isomerase domain of <jats:italic>S. aureus<\/jats:italic> PrsA (PrsA-PPIase). The results of substrate peptide titrations pinpoint the active site and demonstrate the substrate preference of the enzyme. With detailed NMR spectroscopic investigation of the orientation and tautomeric state of the active site histidines we are able to give further insight into the structure of the catalytic site. NMR relaxation analysis gives information on the dynamic behaviour of PrsA-PPIase.<\/jats:p>\n          <\/jats:sec>\n          <jats:sec>\n            <jats:title>Conclusion<\/jats:title>\n            <jats:p>Detailed structural description of the <jats:italic>S. aureus<\/jats:italic> PrsA-PPIase lays the foundation for structure-based design of enzyme inhibitors. The structure resembles hPin1-type parvulins both structurally and regarding substrate preference. Even though a wealth of structural data is available on parvulins, the catalytic mechanism has yet to be resolved. The structure of <jats:italic>S. aureus<\/jats:italic> PrsA-PPIase and our findings on the role of the conserved active site histidines help in designing further experiments to solve the detailed catalytic mechanism.<\/jats:p>\n          <\/jats:sec>","DOI":"10.1186\/1472-6807-9-17","type":"journal-article","created":{"date-parts":[[2009,3,24]],"date-time":"2009-03-24T19:13:07Z","timestamp":1237921987000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":39,"title":["Solution structure of the parvulin-type PPIase domain of Staphylococcus aureus PrsA \u2013 Implications for the catalytic mechanism of parvulins"],"prefix":"10.1186","volume":"9","author":[{"given":"Outi","family":"Heikkinen","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Raili","family":"Seppala","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Helena","family":"Tossavainen","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sami","family":"Heikkinen","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Harri","family":"Koskela","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Perttu","family":"Permi","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ilkka","family":"Kilpel\u00e4inen","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","published-online":{"date-parts":[[2009,3,24]]},"reference":[{"key":"237_CR1","doi-asserted-by":"publisher","first-page":"1225","DOI":"10.1016\/S0140-6736(00)04403-2","volume":"357","author":"M Kuroda","year":"2001","unstructured":"Kuroda M, Ohta T, Uchiyama I, Baba T, Yuzawa H, Kobayashi I, Cui L, Oguchi A, Aoki K, Nagai Y, Lian J, Ito T, Kanamori M, Matsumaru H, Maruyama A, Murakami H, Hosoyama A, Mizutani-Ui Y, Takahashi NK, Sawano T, Inoue R, Kaito C, Sekimizu K, Hirakawa H, Kuhara S, Goto S, Yabuzaki J, Kanehisa M, Yamashita A, Oshima K, Furuya K, Yoshino C, Shiba T, Hattori M, Ogasawara N, Hayashi H, Hiramatsu K: Whole genome sequencing of meticillin-resistant Staphylococcus aureus . 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