Structural basis for enantiomer binding and separation of a common beta-blocker: Crystal structure of cellobiohydrolase Cel7A with bound (S)-propranolol at 1.9 angstrom resolution

Jerry Ståhlberg; Hongbin Henriksson; Christina Divne; Roland Isaksson; Göran Pettersson; Gunnar Johansson; T. Alwyn Jones

doi:10.1006/jmbi.2000.4237

Structural basis for enantiomer binding and separation of a common beta-blocker: Crystal structure of cellobiohydrolase Cel7A with bound (S)-propranolol at 1.9 angstrom resolution

Jerry Ståhlberg
, Hongbin Henriksson
, Christina Divne
, Roland Isaksson
, Göran Pettersson
, Gunnar Johansson
, T. Alwyn Jones

Publikation: Bidrag till tidskrift › Artikel i vetenskaplig tidskrift › Peer review

Sammanfattning

By using cellobiose as a selective competing ligand, the retention of the enantiomers of propranolol on the chiral stationary phase (CSP) based on Cel7A mutant D214N were resolved into enantioselective and non-selective binding. The enantioselective binding was weaker for both enantiomers on D214N-CSP than on wild-type-CSP. (C) 2001 Academic Press.

Originalspråk	Engelska
Sidor (från-till)	79-93
Antal sidor	15
Tidskrift	Journal of Molecular Biology
Volym	305
Nummer	1
DOI	https://doi.org/10.1006/jmbi.2000.4237
Status	Publicerad - 2001
Externt publicerad	Ja

Nyckelord

cellobiohydrolase
cellulase
chiral separation
crystal structure
enantiomer

Åtkomst av dokument

10.1006/jmbi.2000.4237

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Ståhlberg, J., Henriksson, H., Divne, C., Isaksson, R., Pettersson, G., Johansson, G., & Jones, T. A. (2001). Structural basis for enantiomer binding and separation of a common beta-blocker: Crystal structure of cellobiohydrolase Cel7A with bound (S)-propranolol at 1.9 angstrom resolution. Journal of Molecular Biology, 305(1), 79-93. https://doi.org/10.1006/jmbi.2000.4237

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title = "Structural basis for enantiomer binding and separation of a common beta-blocker: Crystal structure of cellobiohydrolase Cel7A with bound (S)-propranolol at 1.9 angstrom resolution",

abstract = "By using cellobiose as a selective competing ligand, the retention of the enantiomers of propranolol on the chiral stationary phase (CSP) based on Cel7A mutant D214N were resolved into enantioselective and non-selective binding. The enantioselective binding was weaker for both enantiomers on D214N-CSP than on wild-type-CSP. (C) 2001 Academic Press.",

keywords = "cellobiohydrolase, cellulase, chiral separation, crystal structure, enantiomer, cellobiohydrolase, cellulase, chiral separation, crystal structure, enantiomer",

author = "Jerry St{\aa}hlberg and Hongbin Henriksson and Christina Divne and Roland Isaksson and G{\"o}ran Pettersson and Gunnar Johansson and Jones, \{T. Alwyn\}",

year = "2001",

doi = "10.1006/jmbi.2000.4237",

language = "English",

volume = "305",

pages = "79--93",

journal = "Journal of Molecular Biology",

issn = "0022-2836",

publisher = "Academic Press",

number = "1",

}

Ståhlberg, J, Henriksson, H, Divne, C, Isaksson, R, Pettersson, G, Johansson, G & Jones, TA 2001, 'Structural basis for enantiomer binding and separation of a common beta-blocker: Crystal structure of cellobiohydrolase Cel7A with bound (S)-propranolol at 1.9 angstrom resolution', Journal of Molecular Biology, vol. 305, nr. 1, s. 79-93. https://doi.org/10.1006/jmbi.2000.4237

Structural basis for enantiomer binding and separation of a common beta-blocker: Crystal structure of cellobiohydrolase Cel7A with bound (S)-propranolol at 1.9 angstrom resolution. / Ståhlberg, Jerry; Henriksson, Hongbin; Divne, Christina et al.
I: Journal of Molecular Biology, Vol. 305, Nr. 1, 2001, s. 79-93.

Publikation: Bidrag till tidskrift › Artikel i vetenskaplig tidskrift › Peer review

TY - JOUR

T1 - Structural basis for enantiomer binding and separation of a common beta-blocker: Crystal structure of cellobiohydrolase Cel7A with bound (S)-propranolol at 1.9 angstrom resolution

AU - Ståhlberg, Jerry

AU - Henriksson, Hongbin

AU - Divne, Christina

AU - Isaksson, Roland

AU - Pettersson, Göran

AU - Johansson, Gunnar

AU - Jones, T. Alwyn

PY - 2001

Y1 - 2001

N2 - By using cellobiose as a selective competing ligand, the retention of the enantiomers of propranolol on the chiral stationary phase (CSP) based on Cel7A mutant D214N were resolved into enantioselective and non-selective binding. The enantioselective binding was weaker for both enantiomers on D214N-CSP than on wild-type-CSP. (C) 2001 Academic Press.

AB - By using cellobiose as a selective competing ligand, the retention of the enantiomers of propranolol on the chiral stationary phase (CSP) based on Cel7A mutant D214N were resolved into enantioselective and non-selective binding. The enantioselective binding was weaker for both enantiomers on D214N-CSP than on wild-type-CSP. (C) 2001 Academic Press.

KW - cellobiohydrolase

KW - cellulase

KW - chiral separation

KW - crystal structure

KW - enantiomer

KW - cellobiohydrolase

KW - cellulase

KW - chiral separation

KW - crystal structure

KW - enantiomer

UR - https://res.slu.se/id/publ/53164

U2 - 10.1006/jmbi.2000.4237

DO - 10.1006/jmbi.2000.4237

M3 - Journal article

C2 - 11114249

SN - 0022-2836

VL - 305

SP - 79

EP - 93

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

IS - 1

ER -