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Preliminary structural studies on the leucine‐zipper homology region of the human protein Bap31

Preliminary structural studies on the leucine‐zipper homology region of the human protein Bap31 B‐cell receptor‐associated protein 31 (Bap31) is an integral membrane protein located in the endoplasmic reticulum (ER) that participates in the transport and quality control of membrane proteins and plays a role in determining cell sensitivity to ER stress and apoptosis. Its cytoplasmic region contains two target sites for caspase cleavage in certain apoptotic pathways. Here, the subcloning, expression, purification and crystallization of the Homo sapiens Bap31 leucine‐zipper C‐terminal fragment, which spans residues Gly160–Glu246, are reported. An N‐terminally His‐tagged protein was overexpressed in Escherichia coli and purified by chromatographic methods. X‐ray diffraction data were collected in‐house to 2.5 Å resolution. Crystals belong to space group P6122/P6522, with unit‐cell parameters a = b = 70.7, c = 80.6 Å. Data analysis indicates the presence of one molecule per asymmetric unit. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Crystallographica Section F Wiley

Preliminary structural studies on the leucine‐zipper homology region of the human protein Bap31

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References (16)

Publisher
Wiley
Copyright
Copyright © 2007 Wiley Subscription Services, Inc., A Wiley Company
ISSN
1744-3091
eISSN
1744-3091
DOI
10.1107/S1744309107008925
pmid
17401199
Publisher site
See Article on Publisher Site

Abstract

B‐cell receptor‐associated protein 31 (Bap31) is an integral membrane protein located in the endoplasmic reticulum (ER) that participates in the transport and quality control of membrane proteins and plays a role in determining cell sensitivity to ER stress and apoptosis. Its cytoplasmic region contains two target sites for caspase cleavage in certain apoptotic pathways. Here, the subcloning, expression, purification and crystallization of the Homo sapiens Bap31 leucine‐zipper C‐terminal fragment, which spans residues Gly160–Glu246, are reported. An N‐terminally His‐tagged protein was overexpressed in Escherichia coli and purified by chromatographic methods. X‐ray diffraction data were collected in‐house to 2.5 Å resolution. Crystals belong to space group P6122/P6522, with unit‐cell parameters a = b = 70.7, c = 80.6 Å. Data analysis indicates the presence of one molecule per asymmetric unit.

Journal

Acta Crystallographica Section F – Wiley

Published: Apr 1, 2007

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