Crystallization of two glutathione S-transferases from an unusual gene family

A. J. Oakley, K. Jirajaroenrat, T. Harnnoi, A. J. Ketterman, M. C.J. Wilce

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

Two glutathione S-transferase isozymes from the mosquito Anopheles dirus (AdGST1-3 and AdGST1-4) from an alternately spliced gene family have been expressed, purified and crystallized. The isozymes share an N-terminal domain derived from a single exon and C-terminal domains from unique exons. Despite the high level of sequence identity (64% overall), the two isozymes crystallize in different space groups, the 1-3 isozyme in P3121 or P3221 (unit-cell parameters a = 49.9, c = 271.8 Å at 100 K) and the 1-4 isozyme in P41 or P43 (unit-cell parameters a = 87.8, c = 166.1 at 100 K). Determination of these structures will advance our understanding of how these enzymes inactivate pesticides and the structural consequences of alternate splicing.

Original languageEnglish
Pages (from-to)870-872
Number of pages3
JournalActa Crystallographica Section D: Biological Crystallography
Volume57
Issue number6
DOIs
Publication statusPublished - Jul 4 2001

Fingerprint

Crystallization
Glutathione Transferase
Isoenzymes
Genes
Exons
Anopheles
Recombinant DNA
Alternative Splicing
Culicidae
Pesticides
Enzymes

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Medicine(all)

Cite this

Crystallization of two glutathione S-transferases from an unusual gene family. / Oakley, A. J.; Jirajaroenrat, K.; Harnnoi, T.; Ketterman, A. J.; Wilce, M. C.J.

In: Acta Crystallographica Section D: Biological Crystallography, Vol. 57, No. 6, 04.07.2001, p. 870-872.

Research output: Contribution to journalArticle

Oakley, A. J. ; Jirajaroenrat, K. ; Harnnoi, T. ; Ketterman, A. J. ; Wilce, M. C.J. / Crystallization of two glutathione S-transferases from an unusual gene family. In: Acta Crystallographica Section D: Biological Crystallography. 2001 ; Vol. 57, No. 6. pp. 870-872.
@article{0b60ce44370d49c1a5792c1bf83a8c2f,
title = "Crystallization of two glutathione S-transferases from an unusual gene family",
abstract = "Two glutathione S-transferase isozymes from the mosquito Anopheles dirus (AdGST1-3 and AdGST1-4) from an alternately spliced gene family have been expressed, purified and crystallized. The isozymes share an N-terminal domain derived from a single exon and C-terminal domains from unique exons. Despite the high level of sequence identity (64{\%} overall), the two isozymes crystallize in different space groups, the 1-3 isozyme in P3121 or P3221 (unit-cell parameters a = 49.9, c = 271.8 {\AA} at 100 K) and the 1-4 isozyme in P41 or P43 (unit-cell parameters a = 87.8, c = 166.1 at 100 K). Determination of these structures will advance our understanding of how these enzymes inactivate pesticides and the structural consequences of alternate splicing.",
author = "Oakley, {A. J.} and K. Jirajaroenrat and T. Harnnoi and Ketterman, {A. J.} and Wilce, {M. C.J.}",
year = "2001",
month = "7",
day = "4",
doi = "10.1107/S0907444901004929",
language = "English",
volume = "57",
pages = "870--872",
journal = "Acta Crystallographica Section D: Structural Biology",
issn = "0907-4449",
publisher = "John Wiley and Sons Inc.",
number = "6",

}

TY - JOUR

T1 - Crystallization of two glutathione S-transferases from an unusual gene family

AU - Oakley, A. J.

AU - Jirajaroenrat, K.

AU - Harnnoi, T.

AU - Ketterman, A. J.

AU - Wilce, M. C.J.

PY - 2001/7/4

Y1 - 2001/7/4

N2 - Two glutathione S-transferase isozymes from the mosquito Anopheles dirus (AdGST1-3 and AdGST1-4) from an alternately spliced gene family have been expressed, purified and crystallized. The isozymes share an N-terminal domain derived from a single exon and C-terminal domains from unique exons. Despite the high level of sequence identity (64% overall), the two isozymes crystallize in different space groups, the 1-3 isozyme in P3121 or P3221 (unit-cell parameters a = 49.9, c = 271.8 Å at 100 K) and the 1-4 isozyme in P41 or P43 (unit-cell parameters a = 87.8, c = 166.1 at 100 K). Determination of these structures will advance our understanding of how these enzymes inactivate pesticides and the structural consequences of alternate splicing.

AB - Two glutathione S-transferase isozymes from the mosquito Anopheles dirus (AdGST1-3 and AdGST1-4) from an alternately spliced gene family have been expressed, purified and crystallized. The isozymes share an N-terminal domain derived from a single exon and C-terminal domains from unique exons. Despite the high level of sequence identity (64% overall), the two isozymes crystallize in different space groups, the 1-3 isozyme in P3121 or P3221 (unit-cell parameters a = 49.9, c = 271.8 Å at 100 K) and the 1-4 isozyme in P41 or P43 (unit-cell parameters a = 87.8, c = 166.1 at 100 K). Determination of these structures will advance our understanding of how these enzymes inactivate pesticides and the structural consequences of alternate splicing.

UR - http://www.scopus.com/inward/record.url?scp=0034979951&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0034979951&partnerID=8YFLogxK

U2 - 10.1107/S0907444901004929

DO - 10.1107/S0907444901004929

M3 - Article

C2 - 11375512

AN - SCOPUS:0034979951

VL - 57

SP - 870

EP - 872

JO - Acta Crystallographica Section D: Structural Biology

JF - Acta Crystallographica Section D: Structural Biology

SN - 0907-4449

IS - 6

ER -