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| Hauptseite > Publikationsdatenbank > The Membrane-Integrated Steric Chaperone Lif Facilitates Active Site Opening of Pseudomonas aeruginosa Lipase A > print |
| Hauptseite > Publikationsdatenbank > The Membrane-Integrated Steric Chaperone Lif Facilitates Active Site Opening of Pseudomonas aeruginosa Lipase A > print |
| 001 | 865808 | ||
| 005 | 20210130003146.0 | ||
| 024 | 7 | _ | |a 10.1002/jcc.26085 |2 doi |
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| 100 | 1 | _ | |a Verma, Neha |0 P:(DE-HGF)0 |b 0 |
| 245 | _ | _ | |a The Membrane-Integrated Steric Chaperone Lif Facilitates Active Site Opening of Pseudomonas aeruginosa Lipase A |
| 260 | _ | _ | |a New York, NY [u.a.] |c 2020 |b Wiley |
| 336 | 7 | _ | |a article |2 DRIVER |
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| 520 | _ | _ | |a Lipases are essential and widely used biocatalysts. Hence, the production of lipases requires a detailed understanding of the molecular mechanism of its folding and secretion. Lipase A from Pseudomonas aeruginosa, PaLipA, constitutes a prominent example that has additional relevance because of its role as a virulence factor in many diseases. PaLipA requires the assistance of a membrane‐integrated steric chaperone, the lipase‐specific foldase Lif, to achieve its enzymatically active state. However, the molecular mechanism of how Lif activates its cognate lipase has remained elusive. Here, we show by molecular dynamics simulations at the atomistic level and potential of mean force computations that Lif catalyzes the activation process of PaLipA by structurally stabilizing an intermediate PaLipA conformation, particularly a β‐sheet in the region of residues 17–30, such that the opening of PaLipA's lid domain is facilitated. This opening allows substrate access to PaLipA's catalytic site. A surprising and so far not fully understood aspect of our study is that the open state of PaLipA is unstable compared to the closed one according to our computational and in vitro biochemical results. We thus speculate that further interactions of PaLipA with the Xcp secretion machinery and/or components of the extracellular matrix contribute to the remaining activity of secreted PaLipA. |
| 536 | _ | _ | |a 511 - Computational Science and Mathematical Methods (POF3-511) |0 G:(DE-HGF)POF3-511 |c POF3-511 |f POF III |x 0 |
| 536 | _ | _ | |a Forschergruppe Gohlke (hkf7_20170501) |0 G:(DE-Juel1)hkf7_20170501 |c hkf7_20170501 |f Forschergruppe Gohlke |x 1 |
| 536 | _ | _ | |a Analysis of the conformational changes during activation of lipase A by its foldase (hdd16_20171101) |0 G:(DE-Juel1)hdd16_20171101 |c hdd16_20171101 |f Analysis of the conformational changes during activation of lipase A by its foldase |x 2 |
| 536 | _ | _ | |a Conformational dynamics of the unbound lipase-specific foldase Lif (hdd16_20161101) |0 G:(DE-Juel1)hdd16_20161101 |c hdd16_20161101 |f Conformational dynamics of the unbound lipase-specific foldase Lif |x 3 |
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| 700 | 1 | _ | |a Jaeger, Karl-Erich |0 P:(DE-Juel1)131457 |b 3 |
| 700 | 1 | _ | |a Gohlke, Holger |0 P:(DE-Juel1)172663 |b 4 |e Corresponding author |
| 773 | _ | _ | |a 10.1002/jcc.26085 |0 PERI:(DE-600)1479181-x |n 6 |p 500-512 |t Journal of computational chemistry |v 4 |y 2020 |x 0192-8651 |
| 856 | 4 | _ | |u https://juser.fz-juelich.de/record/865808/files/Verma_et_al-2020-Journal_of_Computational_Chemistry.pdf |y Restricted |
| 856 | 4 | _ | |y Published on 2019-10-16. Available in OpenAccess from 2020-10-16. |u https://juser.fz-juelich.de/record/865808/files/PMF_LifLipA_manuscript_final_rev2_final.pdf |
| 856 | 4 | _ | |y Published on 2019-10-16. Available in OpenAccess from 2020-10-16. |x pdfa |u https://juser.fz-juelich.de/record/865808/files/PMF_LifLipA_manuscript_final_rev2_final.pdf?subformat=pdfa |
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