PDBsum entry 1v2a

Transferase

PDB id

1v2a

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Contents

			Protein chains

					208 a.a. *

			Ligands

					GTS ×4

			Waters ×208

* Residue conservation analysis

PDB id:

1v2a

Links

Name:

Transferase

Title:

Glutathione s-transferase 1-6 from anopheles dirus species b

Structure:

Glutathione transferase gst1-6. Chain: a, b, c, d. Synonym: glutathione s-transferase 1-6. Engineered: yes

Source:

Anopheles dirus. Organism_taxid: 7168. Gene: adgst1-6. Expressed in: escherichia coli. Expression_system_taxid: 562

Biol. unit:

Dimer (from PQS)

Resolution:

2.15Å

R-factor:

0.234

R-free:

0.284

Authors:

A.J.Oakley

Key ref:

R.Udomsinprasert et al. (2005). Identification, characterization and structure of a new Delta class glutathione transferase isoenzyme. Biochem J, 388, 763-771. PubMed id: 15717864

Date:

10-Oct-03

Release date:

28-Oct-03

PROCHECK

	Headers

	References

Protein chains

Q9BHB0 (Q9BHB0_9DIPT) - Glutathione transferase gst1-6 from Anopheles dirus

Seq: Struc:					210 a.a. 208 a.a.

Key:

PfamA domain

Secondary structure

CATH domain



		Enzyme reactions

Enzyme class:

E.C.2.5.1.18 - glutathione transferase.

[IntEnz] [ExPASy] [KEGG] [BRENDA]

Reaction:

RX + glutathione = an S-substituted glutathione + a halide anion + H⁺

RX
Bound ligand (Het Group name = GTS)
matches with 86.96% similarity

glutathione

S-substituted glutathione

halide anion

H(+)

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

Added reference

	Biochem J 388:763-771 (2005)
PubMed id: 15717864

Identification, characterization and structure of a new Delta class glutathione transferase isoenzyme.
R.Udomsinprasert, S.Pongjaroenkit, J.Wongsantichon, A.J.Oakley, L.A.Prapanthadara, M.C.Wilce, A.J.Ketterman.

ABSTRACT

The insect GST (glutathione transferase) supergene family encodes a varied group of proteins belonging to at least six individual classes. Interest in insect GSTs has focused on their role in conferring insecticide resistance. Previously from the mosquito malaria vector Anopheles dirus, two genes encoding five Delta class GSTs have been characterized for structural as well as enzyme activities. We have obtained a new Delta class GST gene and isoenzyme from A. dirus, which we name adGSTD5-5. The adGSTD5-5 isoenzyme was identified and was only detectably expressed in A. dirus adult females. A putative promoter analysis suggests that this GST has an involvement in oogenesis. The enzyme displayed little activity for classical GST substrates, although it possessed the greatest activity for DDT [1,1,1-trichloro-2,2-bis-(p-chlorophenyl)ethane] observed for Delta GSTs. However, GST activity was inhibited or enhanced in the presence of various fatty acids, suggesting that the enzyme may be modulated by fatty acids. We obtained a crystal structure for adGSTD5-5 and compared it with other Delta GSTs, which showed that adGSTD5-5 possesses an elongated and more polar active-site topology.

Literature references that cite this PDB file's key reference

PubMed id

Reference

19052367

E.H.Jang, H.Park, A.K.Park, J.H.Moon, Y.M.Chi, and I.Y.Ahn (2008).
Crystallization and preliminary X-ray crystallographic studies of the rho-class glutathione S-transferase from the Antarctic clam Laternula elliptica.

Acta Crystallogr Sect F Struct Biol Cryst Commun, 64, 1132-1134.

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.