Crystallographic structure and molecular dynamics simulations of the major endoglucanase from Xanthomonas campestris pv. campestris shed light on its oligosaccharide products release pattern
Authorized Users Only
2019
Authors
Puhl, Ana C.Prates, Erica T.
Rosseto, Flávio R.
Manzine, Livia R.
Stanković, Ivana
de Araújo, Simara S.
Alvarez, Thabata M.
Squina, Fábio M.
Skaf, Munir S.
Polikarpov, Igor
Article (Published version)
Metadata
Show full item recordAbstract
Cellulases are essential enzymatic components for the transformation of plant biomass into fuels, renewable ma-
terials and green chemicals. Here, we determined the crystal structure, pattern of hydrolysis products release,
and conducted molecular dynamics simulations of the major endoglucanase from the Xanthomonas campestris
pv. campestris (XccCel5A). XccCel5A has a TIM barrel fold with the catalytic site centrally placed in a binding
groove surrounded by aromatic side chains. Molecular dynamics simulations show that productive position of
the substrate is secured by a network of hydrogen bonds in the four main subsites, which differ in details from
homologous structures. Capillary zone electrophoresis and computational studies reveal XccCel5A can act both
as endoglucanase and licheninase, but there are preferable arrangements of substrate regarding β-1,3 and β-
1,4 bonds within the binding cleft which are related to the enzymatic efficiency.
Keywords:
Endoglucanase / Molecular dynamics / X-ray structureSource:
International Journal of Biological Macromolecules, 2019, 136, 493-502Publisher:
- Elsevier B.V.
Funding / projects:
- Fundação de Amparo a Pesquisa do Estado de São Paulo (FAPESP) grant 10/52362-5
- Fundação de Amparo a Pesquisa do Estado de São Paulo (FAPESP) grant 11/20505-4
- Fundação de Amparo a Pesquisa do Estado de São Paulo (FAPESP) grant 11/ 21608-1
- Fundação de Amparo a Pesquisa do Estado de São Paulo (FAPESP) grant 15/50590-4
- Fundação de Amparo a Pesquisa do Estado de São Paulo (FAPESP) grant 15/13684-0
- INCT Bioetanol (FAPESP/CNPq)
- Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq) grant 405191/2015-4
- Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq) grant 303988/2016-9
- Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq) grant 440977/2016-9
- Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq) grant 151963/2018-5
- MCT/CNPq/FAPESP EU-Brazil Collaboration program in Second Generation Biofuels (CeProBio Project; FAPESP 2009/52840-7 and CNPq 490022/2009-0)
DOI: 10.1016/j.ijbiomac.2019.06.107
ISSN: 0141-8130
PubMed: 0141-8130
Scopus: 2-s2.0-85067429708
Institution/Community
IHTMTY - JOUR AU - Puhl, Ana C. AU - Prates, Erica T. AU - Rosseto, Flávio R. AU - Manzine, Livia R. AU - Stanković, Ivana AU - de Araújo, Simara S. AU - Alvarez, Thabata M. AU - Squina, Fábio M. AU - Skaf, Munir S. AU - Polikarpov, Igor PY - 2019 UR - https://cer.ihtm.bg.ac.rs/handle/123456789/6083 AB - Cellulases are essential enzymatic components for the transformation of plant biomass into fuels, renewable ma- terials and green chemicals. Here, we determined the crystal structure, pattern of hydrolysis products release, and conducted molecular dynamics simulations of the major endoglucanase from the Xanthomonas campestris pv. campestris (XccCel5A). XccCel5A has a TIM barrel fold with the catalytic site centrally placed in a binding groove surrounded by aromatic side chains. Molecular dynamics simulations show that productive position of the substrate is secured by a network of hydrogen bonds in the four main subsites, which differ in details from homologous structures. Capillary zone electrophoresis and computational studies reveal XccCel5A can act both as endoglucanase and licheninase, but there are preferable arrangements of substrate regarding β-1,3 and β- 1,4 bonds within the binding cleft which are related to the enzymatic efficiency. PB - Elsevier B.V. T2 - International Journal of Biological Macromolecules T1 - Crystallographic structure and molecular dynamics simulations of the major endoglucanase from Xanthomonas campestris pv. campestris shed light on its oligosaccharide products release pattern VL - 136 SP - 493 EP - 502 DO - 10.1016/j.ijbiomac.2019.06.107 ER -
@article{ author = "Puhl, Ana C. and Prates, Erica T. and Rosseto, Flávio R. and Manzine, Livia R. and Stanković, Ivana and de Araújo, Simara S. and Alvarez, Thabata M. and Squina, Fábio M. and Skaf, Munir S. and Polikarpov, Igor", year = "2019", abstract = "Cellulases are essential enzymatic components for the transformation of plant biomass into fuels, renewable ma- terials and green chemicals. Here, we determined the crystal structure, pattern of hydrolysis products release, and conducted molecular dynamics simulations of the major endoglucanase from the Xanthomonas campestris pv. campestris (XccCel5A). XccCel5A has a TIM barrel fold with the catalytic site centrally placed in a binding groove surrounded by aromatic side chains. Molecular dynamics simulations show that productive position of the substrate is secured by a network of hydrogen bonds in the four main subsites, which differ in details from homologous structures. Capillary zone electrophoresis and computational studies reveal XccCel5A can act both as endoglucanase and licheninase, but there are preferable arrangements of substrate regarding β-1,3 and β- 1,4 bonds within the binding cleft which are related to the enzymatic efficiency.", publisher = "Elsevier B.V.", journal = "International Journal of Biological Macromolecules", title = "Crystallographic structure and molecular dynamics simulations of the major endoglucanase from Xanthomonas campestris pv. campestris shed light on its oligosaccharide products release pattern", volume = "136", pages = "493-502", doi = "10.1016/j.ijbiomac.2019.06.107" }
Puhl, A. C., Prates, E. T., Rosseto, F. R., Manzine, L. R., Stanković, I., de Araújo, S. S., Alvarez, T. M., Squina, F. M., Skaf, M. S.,& Polikarpov, I.. (2019). Crystallographic structure and molecular dynamics simulations of the major endoglucanase from Xanthomonas campestris pv. campestris shed light on its oligosaccharide products release pattern. in International Journal of Biological Macromolecules Elsevier B.V.., 136, 493-502. https://doi.org/10.1016/j.ijbiomac.2019.06.107
Puhl AC, Prates ET, Rosseto FR, Manzine LR, Stanković I, de Araújo SS, Alvarez TM, Squina FM, Skaf MS, Polikarpov I. Crystallographic structure and molecular dynamics simulations of the major endoglucanase from Xanthomonas campestris pv. campestris shed light on its oligosaccharide products release pattern. in International Journal of Biological Macromolecules. 2019;136:493-502. doi:10.1016/j.ijbiomac.2019.06.107 .
Puhl, Ana C., Prates, Erica T., Rosseto, Flávio R., Manzine, Livia R., Stanković, Ivana, de Araújo, Simara S., Alvarez, Thabata M., Squina, Fábio M., Skaf, Munir S., Polikarpov, Igor, "Crystallographic structure and molecular dynamics simulations of the major endoglucanase from Xanthomonas campestris pv. campestris shed light on its oligosaccharide products release pattern" in International Journal of Biological Macromolecules, 136 (2019):493-502, https://doi.org/10.1016/j.ijbiomac.2019.06.107 . .