Large scale structural rearrangement of a serine hydrolase from francisella tularensis facilitates catalysis

Ekaterina V. Filippova; Leigh A. Weston; Misty L. Kuhn; Brett Geissler; Alexandra M. Gehring; Nicola Armoush; Chinessa T. Adkins; George Minasov; Ievgeniia Dubrovska; Ludmilla Shuvalova; James R. Winsor; Luke D. Lavis; Karla J F Satchell; Daniel P. Becker; Wayne F. Anderson; R. Jeremy Johnson

doi:10.1074/jbc.M112.446625

Large scale structural rearrangement of a serine hydrolase from francisella tularensis facilitates catalysis

Ekaterina V. Filippova, Leigh A. Weston, Misty L. Kuhn, Brett Geissler, Alexandra M. Gehring, Nicola Armoush, Chinessa T. Adkins, George Minasov, Ievgeniia Dubrovska, Ludmilla Shuvalova, James R. Winsor, Luke D. Lavis, Karla J F Satchell, Daniel P. Becker, Wayne F. Anderson, R. Jeremy Johnson^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

28 Scopus citations

Abstract

Background: Acyl protein thioesterases control protein S-acylation at cellular membranes. Results: FTT258 is a serine hydrolase with broad substrate specificity that binds to bacterial membranes and exists in two distinct conformations. Conclusion: Conformational changes in FTT258 are correlated with catalytic activity. Significance: Structural rearrangement dually regulates the membrane binding and catalytic activity of acyl protein thioesterases.

Original language	English (US)
Pages (from-to)	10522-10535
Number of pages	14
Journal	Journal of Biological Chemistry
Volume	288
Issue number	15
DOIs	https://doi.org/10.1074/jbc.M112.446625
State	Published - Apr 12 2013

ASJC Scopus subject areas

Molecular Biology
Biochemistry
Cell Biology

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10.1074/jbc.M112.446625

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Filippova, E. V., Weston, L. A., Kuhn, M. L., Geissler, B., Gehring, A. M., Armoush, N., Adkins, C. T., Minasov, G., Dubrovska, I., Shuvalova, L., Winsor, J. R., Lavis, L. D., Satchell, K. J. F., Becker, D. P., Anderson, W. F., & Johnson, R. J. (2013). Large scale structural rearrangement of a serine hydrolase from francisella tularensis facilitates catalysis. Journal of Biological Chemistry, 288(15), 10522-10535. https://doi.org/10.1074/jbc.M112.446625

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title = "Large scale structural rearrangement of a serine hydrolase from francisella tularensis facilitates catalysis",

abstract = "Background: Acyl protein thioesterases control protein S-acylation at cellular membranes. Results: FTT258 is a serine hydrolase with broad substrate specificity that binds to bacterial membranes and exists in two distinct conformations. Conclusion: Conformational changes in FTT258 are correlated with catalytic activity. Significance: Structural rearrangement dually regulates the membrane binding and catalytic activity of acyl protein thioesterases.",

author = "Filippova, {Ekaterina V.} and Weston, {Leigh A.} and Kuhn, {Misty L.} and Brett Geissler and Gehring, {Alexandra M.} and Nicola Armoush and Adkins, {Chinessa T.} and George Minasov and Ievgeniia Dubrovska and Ludmilla Shuvalova and Winsor, {James R.} and Lavis, {Luke D.} and Satchell, {Karla J F} and Becker, {Daniel P.} and Anderson, {Wayne F.} and Johnson, {R. Jeremy}",

year = "2013",

month = apr,

day = "12",

doi = "10.1074/jbc.M112.446625",

language = "English (US)",

volume = "288",

pages = "10522--10535",

journal = "Journal of Biological Chemistry",

issn = "0021-9258",

publisher = "American Society for Biochemistry and Molecular Biology Inc.",

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Filippova, EV, Weston, LA, Kuhn, ML, Geissler, B, Gehring, AM, Armoush, N, Adkins, CT, Minasov, G, Dubrovska, I, Shuvalova, L, Winsor, JR, Lavis, LD, Satchell, KJF, Becker, DP, Anderson, WF & Johnson, RJ 2013, 'Large scale structural rearrangement of a serine hydrolase from francisella tularensis facilitates catalysis', Journal of Biological Chemistry, vol. 288, no. 15, pp. 10522-10535. https://doi.org/10.1074/jbc.M112.446625

TY - JOUR

T1 - Large scale structural rearrangement of a serine hydrolase from francisella tularensis facilitates catalysis

AU - Filippova, Ekaterina V.

AU - Weston, Leigh A.

AU - Kuhn, Misty L.

AU - Geissler, Brett

AU - Gehring, Alexandra M.

AU - Armoush, Nicola

AU - Adkins, Chinessa T.

AU - Minasov, George

AU - Dubrovska, Ievgeniia

AU - Shuvalova, Ludmilla

AU - Winsor, James R.

AU - Lavis, Luke D.

AU - Satchell, Karla J F

AU - Becker, Daniel P.

AU - Anderson, Wayne F.

AU - Johnson, R. Jeremy

PY - 2013/4/12

Y1 - 2013/4/12

N2 - Background: Acyl protein thioesterases control protein S-acylation at cellular membranes. Results: FTT258 is a serine hydrolase with broad substrate specificity that binds to bacterial membranes and exists in two distinct conformations. Conclusion: Conformational changes in FTT258 are correlated with catalytic activity. Significance: Structural rearrangement dually regulates the membrane binding and catalytic activity of acyl protein thioesterases.

AB - Background: Acyl protein thioesterases control protein S-acylation at cellular membranes. Results: FTT258 is a serine hydrolase with broad substrate specificity that binds to bacterial membranes and exists in two distinct conformations. Conclusion: Conformational changes in FTT258 are correlated with catalytic activity. Significance: Structural rearrangement dually regulates the membrane binding and catalytic activity of acyl protein thioesterases.

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U2 - 10.1074/jbc.M112.446625

DO - 10.1074/jbc.M112.446625

M3 - Article

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AN - SCOPUS:84876228435

SN - 0021-9258

VL - 288

SP - 10522

EP - 10535

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 15

ER -

Large scale structural rearrangement of a serine hydrolase from francisella tularensis facilitates catalysis

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Crystal structure of carboxylesterase/phospholipase family protein from Francisella tularensis

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Large scale structural rearrangement of a serine hydrolase from francisella tularensis facilitates catalysis

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Datasets

Crystal structure of carboxylesterase/phospholipase family protein from Francisella tularensis

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