This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1aw9

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1aw9.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1aw9.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1aw9| PDB=1aw9 | SCENE= }}
{{STRUCTURE_1aw9| PDB=1aw9 | SCENE= }}
-
'''STRUCTURE OF GLUTATHIONE S-TRANSFERASE III IN APO FORM'''
+
===STRUCTURE OF GLUTATHIONE S-TRANSFERASE III IN APO FORM===
-
==Overview==
+
<!--
-
Glutathione S-transferases (GSTs) are enzymes that inactivate toxic compounds by conjugation with glutathione and are involved in resistance towards drugs, antibiotics, insecticides and herbicides. Their ability to confer herbicide tolerance in plants provides a tool to control weeds in a wide variety of agronomic crops. GST-III was prepared from Zea mays var. mutin and its amino acid sequence was determined from two sets of peptides obtained by cleavage with endoprotease Asp-N and with trypsin, respectively. Recombinant GST-III was prepared by extraction of mRNA from plant tissue, transcription into cDNA, amplification by PCR and expression. It was crystallized and the crystal structure of the unligated form was determined at 2.2 A resolution. The enzyme forms a GST-typical dimer with one subunit consisting of 220 residues. Each subunit is formed of two distinct domains, an N-terminal domain consisting of a beta-sheet flanked by two helices, and a C-terminal domain, entirely helical. The dimeric molecule is globular with a large cleft between the two subunits. The amino acid sequence of GST-III and its cDNA sequence determined here show differences from sequences published earlier.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9417936}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9417936 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9417936}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Herbicide detoxification]]
[[Category: Herbicide detoxification]]
[[Category: Transferase]]
[[Category: Transferase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:46:20 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:44:14 2008''

Revision as of 14:44, 30 June 2008

Image:1aw9.png

Template:STRUCTURE 1aw9

STRUCTURE OF GLUTATHIONE S-TRANSFERASE III IN APO FORM

Template:ABSTRACT PUBMED 9417936

About this Structure

1AW9 is a Single protein structure of sequence from Zea mays. Full crystallographic information is available from OCA.

Reference

Cloning, sequencing, crystallization and X-ray structure of glutathione S-transferase-III from Zea mays var. mutin: a leading enzyme in detoxification of maize herbicides., Neuefeind T, Huber R, Reinemer P, Knablein J, Prade L, Mann K, Bieseler B, J Mol Biol. 1997 Dec 12;274(4):577-87. PMID:9417936

Page seeded by OCA on Mon Jun 30 17:44:14 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1aw9"
Personal tools