Structure and Dynamics of a Promiscuous Xanthan Lyase from Paenibacillus nanensis and the Design of Variants with Increased Stability and Activity

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Structure and Dynamics of a Promiscuous Xanthan Lyase from Paenibacillus nanensis and the Design of Variants with Increased Stability and Activity. / Jensen, Pernille Foged; Kadziola, Anders; Comamala, Gerard; Segura, Dorotea R; Anderson, Lars; Poulsen, Jens-Christian N; Rasmussen, Kim Krighaar; Agarwal, Shilpi; Sainathan, Rajendra K; Monrad, Rune Nygaard; Svendsen, Allan; Nielsen, Jens Erik; Lo Leggio, Leila; Rand, Kasper D.

I: Cell Chemical Biology, Bind 26, Nr. 2, 2019, s. 191-202.e1-e6.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Jensen, PF, Kadziola, A, Comamala, G, Segura, DR, Anderson, L, Poulsen, J-CN, Rasmussen, KK, Agarwal, S, Sainathan, RK, Monrad, RN, Svendsen, A, Nielsen, JE, Lo Leggio, L & Rand, KD 2019, 'Structure and Dynamics of a Promiscuous Xanthan Lyase from Paenibacillus nanensis and the Design of Variants with Increased Stability and Activity', Cell Chemical Biology, bind 26, nr. 2, s. 191-202.e1-e6. https://doi.org/10.1016/j.chembiol.2018.10.016

APA

Jensen, P. F., Kadziola, A., Comamala, G., Segura, D. R., Anderson, L., Poulsen, J-C. N., Rasmussen, K. K., Agarwal, S., Sainathan, R. K., Monrad, R. N., Svendsen, A., Nielsen, J. E., Lo Leggio, L., & Rand, K. D. (2019). Structure and Dynamics of a Promiscuous Xanthan Lyase from Paenibacillus nanensis and the Design of Variants with Increased Stability and Activity. Cell Chemical Biology, 26(2), 191-202.e1-e6. https://doi.org/10.1016/j.chembiol.2018.10.016

Vancouver

Jensen PF, Kadziola A, Comamala G, Segura DR, Anderson L, Poulsen J-CN o.a. Structure and Dynamics of a Promiscuous Xanthan Lyase from Paenibacillus nanensis and the Design of Variants with Increased Stability and Activity. Cell Chemical Biology. 2019;26(2):191-202.e1-e6. https://doi.org/10.1016/j.chembiol.2018.10.016

Author

Jensen, Pernille Foged ; Kadziola, Anders ; Comamala, Gerard ; Segura, Dorotea R ; Anderson, Lars ; Poulsen, Jens-Christian N ; Rasmussen, Kim Krighaar ; Agarwal, Shilpi ; Sainathan, Rajendra K ; Monrad, Rune Nygaard ; Svendsen, Allan ; Nielsen, Jens Erik ; Lo Leggio, Leila ; Rand, Kasper D. / Structure and Dynamics of a Promiscuous Xanthan Lyase from Paenibacillus nanensis and the Design of Variants with Increased Stability and Activity. I: Cell Chemical Biology. 2019 ; Bind 26, Nr. 2. s. 191-202.e1-e6.

Bibtex

@article{200cd22dd9dc43a682ee9be7b73aaa65,

title = "Structure and Dynamics of a Promiscuous Xanthan Lyase from Paenibacillus nanensis and the Design of Variants with Increased Stability and Activity",

abstract = "We have characterized the structure and dynamics of the carbohydrate-modifying enzyme Paenibacillus nanensis xanthan lyase (PXL) involved in the degradation of xanthan by X-ray crystallography, small-angle X-ray scattering, and hydrogen/deuterium exchange mass spectrometry. Unlike other xanthan lyases, PXL is specific for both unmodified mannose and pyruvylated mannose, which we find is correlated with structural differences in the substrate binding groove. The structure of the full-length enzyme reveals two additional C-terminal modules, one of which belongs to a new non-catalytic carbohydrate binding module family. Ca2+ are critical for the activity and conformation of PXL, and we show that their removal by chelating agents results in localized destabilization/unfolding of particularly the C-terminal modules. We use the structure and the revealed impact of Ca2+ coordination on conformational dynamics to guide the engineering of PXL variants with increased activity and stability in a chelating environment, thus expanding the possibilities for industrial applications of PXL.",

author = "Jensen, {Pernille Foged} and Anders Kadziola and Gerard Comamala and Segura, {Dorotea R} and Lars Anderson and Poulsen, {Jens-Christian N} and Rasmussen, {Kim Krighaar} and Shilpi Agarwal and Sainathan, {Rajendra K} and Monrad, {Rune Nygaard} and Allan Svendsen and Nielsen, {Jens Erik} and {Lo Leggio}, Leila and Rand, {Kasper D}",

year = "2019",

doi = "10.1016/j.chembiol.2018.10.016",

language = "English",

volume = "26",

pages = "191--202.e1--e6",

journal = "Chemistry and Biology",

issn = "2451-9456",

publisher = "Elsevier",

number = "2",

}

RIS

TY - JOUR

T1 - Structure and Dynamics of a Promiscuous Xanthan Lyase from Paenibacillus nanensis and the Design of Variants with Increased Stability and Activity

AU - Jensen, Pernille Foged

AU - Kadziola, Anders

AU - Comamala, Gerard

AU - Segura, Dorotea R

AU - Anderson, Lars

AU - Poulsen, Jens-Christian N

AU - Rasmussen, Kim Krighaar

AU - Agarwal, Shilpi

AU - Sainathan, Rajendra K

AU - Monrad, Rune Nygaard

AU - Svendsen, Allan

AU - Nielsen, Jens Erik

AU - Lo Leggio, Leila

AU - Rand, Kasper D

PY - 2019

Y1 - 2019

N2 - We have characterized the structure and dynamics of the carbohydrate-modifying enzyme Paenibacillus nanensis xanthan lyase (PXL) involved in the degradation of xanthan by X-ray crystallography, small-angle X-ray scattering, and hydrogen/deuterium exchange mass spectrometry. Unlike other xanthan lyases, PXL is specific for both unmodified mannose and pyruvylated mannose, which we find is correlated with structural differences in the substrate binding groove. The structure of the full-length enzyme reveals two additional C-terminal modules, one of which belongs to a new non-catalytic carbohydrate binding module family. Ca2+ are critical for the activity and conformation of PXL, and we show that their removal by chelating agents results in localized destabilization/unfolding of particularly the C-terminal modules. We use the structure and the revealed impact of Ca2+ coordination on conformational dynamics to guide the engineering of PXL variants with increased activity and stability in a chelating environment, thus expanding the possibilities for industrial applications of PXL.

AB - We have characterized the structure and dynamics of the carbohydrate-modifying enzyme Paenibacillus nanensis xanthan lyase (PXL) involved in the degradation of xanthan by X-ray crystallography, small-angle X-ray scattering, and hydrogen/deuterium exchange mass spectrometry. Unlike other xanthan lyases, PXL is specific for both unmodified mannose and pyruvylated mannose, which we find is correlated with structural differences in the substrate binding groove. The structure of the full-length enzyme reveals two additional C-terminal modules, one of which belongs to a new non-catalytic carbohydrate binding module family. Ca2+ are critical for the activity and conformation of PXL, and we show that their removal by chelating agents results in localized destabilization/unfolding of particularly the C-terminal modules. We use the structure and the revealed impact of Ca2+ coordination on conformational dynamics to guide the engineering of PXL variants with increased activity and stability in a chelating environment, thus expanding the possibilities for industrial applications of PXL.

U2 - 10.1016/j.chembiol.2018.10.016

DO - 10.1016/j.chembiol.2018.10.016

M3 - Journal article

C2 - 30503284

VL - 26

SP - 191-202.e1-e6

JO - Chemistry and Biology

JF - Chemistry and Biology

SN - 2451-9456

IS - 2

ER -

ID: 216348637