Structures of herbicides in complex with their detoxifying enzyme glutathione S- transferase – explanations for the selectivity of the enzyme in plants 

Slides:



Advertisements
Similar presentations
Figure S1: A) Schematic representation of minimal α/β hydrolase fold observed in the structure of bMGL; B) Schematic representation of canonical α/β hydrolase.
Advertisements

Elena Conti, Nick P Franks, Peter Brick  Structure 
Volume 10, Issue 8, Pages (August 2002)
Volume 6, Issue 2, Pages (February 1998)
Crystal Structure of the Tandem Phosphatase Domains of RPTP LAR
Volume 6, Issue 7, Pages (July 1998)
Volume 10, Issue 8, Pages (August 2002)
Crystal structure of Vibrio cholerae neuraminidase reveals dual lectin-like domains in addition to the catalytic domain  Susan Crennell, Elspeth Garman,
Volume 8, Issue 9, Pages (September 2000)
Volume 8, Issue 7, Pages (July 2000)
Volume 5, Issue 1, Pages (January 1997)
Crystal structure of Vibrio cholerae neuraminidase reveals dual lectin-like domains in addition to the catalytic domain  Susan Crennell, Elspeth Garman,
Crystal Structures of a Ligand-free and Malonate-Bound Human Caspase-1
Barley lipid-transfer protein complexed with palmitoyl CoA: the structure reveals a hydrophobic binding site that can expand to fit both large and small.
Volume 3, Issue 12, Pages (December 1995)
Volume 3, Issue 11, Pages (November 1995)
Volume 6, Issue 8, Pages (August 1998)
Volume 8, Issue 12, Pages (December 2001)
Volume 3, Issue 11, Pages (November 1995)
Glycerol Dehydrogenase
Volume 12, Issue 6, Pages (June 2004)
The three-dimensional structure of PNGase F, a glycosyl asparaginase from Flavobacterium meningosepticum  Gillian E Norris, Timothy J Stillman, Bryan.
Volume 8, Issue 3, Pages (March 2000)
Catalytic Center Assembly of HPPK as Revealed by the Crystal Structure of a Ternary Complex at 1.25 Å Resolution  Jaroslaw Blaszczyk, Genbin Shi, Honggao.
Volume 7, Issue 2, Pages (February 1999)
Volume 4, Issue 11, Pages (November 1996)
Crystal Structures of Ral-GppNHp and Ral-GDP Reveal Two Binding Sites that Are Also Present in Ras and Rap  Nathan I. Nicely, Justin Kosak, Vesna de Serrano,
Volume 8, Issue 8, Pages (August 2000)
Volume 3, Issue 2, Pages (February 1995)
The Monomeric dUTPase from Epstein-Barr Virus Mimics Trimeric dUTPases
Volume 8, Issue 9, Pages (September 2000)
The 1.8 Å crystal structure of catechol 1,2-dioxygenase reveals a novel hydrophobic helical zipper as a subunit linker  Matthew W Vetting, Douglas H Ohlendorf 
Volume 95, Issue 7, Pages (December 1998)
Edith Schlagenhauf, Robert Etges, Peter Metcalf  Structure 
Volume 5, Issue 1, Pages (January 1997)
The sequence, crystal structure determination and refinement of two crystal forms of lipase B from Candida antarctica  Jonas Uppenberg, Mogens Trier Hansen,
Crystal Structure of Carnitine Acetyltransferase and Implications for the Catalytic Mechanism and Fatty Acid Transport  Gerwald Jogl, Liang Tong  Cell 
Volume 6, Issue 3, Pages (March 1998)
Crystal structure of the ternary complex of 1,3,8-trihydroxynaphthalene reductase from Magnaporthe grisea with NADPH and an active-site inhibitor  Arnold.
Volume 5, Issue 2, Pages (February 1997)
The basis for K-Ras4B binding specificity to protein farnesyl-transferase revealed by 2 Å resolution ternary complex structures  Stephen B Long, Patrick.
Volume 5, Issue 3, Pages (March 1997)
Volume 2, Issue 5, Pages (May 1994)
The structure of the C-terminal domain of methionine synthase: presenting S- adenosylmethionine for reductive methylation of B12  Melinda M Dixon, Sha.
Crystal Structure of Saccharopine Reductase from Magnaporthe grisea, an Enzyme of the α-Aminoadipate Pathway of Lysine Biosynthesis  Eva Johansson, James.
Elena Conti, Nick P Franks, Peter Brick  Structure 
Volume 11, Issue 12, Pages (December 2003)
Volume 7, Issue 7, Pages (July 2000)
How glutaminyl-tRNA synthetase selects glutamine
Volume 7, Issue 8, Pages (August 1999)
Volume 7, Issue 9, Pages (September 1999)
Volume 3, Issue 6, Pages (June 1995)
Volume 3, Issue 9, Pages (September 1995)
Volume 5, Issue 10, Pages (October 1997)
Volume 7, Issue 5, Pages (May 1999)
Volume 5, Issue 10, Pages (October 1997)
The crystal structure of an intact human Max–DNA complex: new insights into mechanisms of transcriptional control  P Brownlie, TA Ceska, M Lamers, C Romier,
Volume 3, Issue 12, Pages (December 1995)
Volume 8, Issue 9, Pages (September 2000)
Volume 10, Issue 4, Pages (April 2003)
Volume 3, Issue 4, Pages (April 1995)
Volume 6, Issue 8, Pages (August 1998)
Volume 7, Issue 12, Pages (January 1999)
Volume 6, Issue 3, Pages (March 1998)
Volume 5, Issue 6, Pages (June 1997)
Crystal Structure of Hyaluronidase, a Major Allergen of Bee Venom
Volume 9, Issue 11, Pages (November 2002)
Volume 4, Issue 6, Pages (June 1996)
Volume 7, Issue 2, Pages (February 1999)
Stanley J Watowich, John J Skehel, Don C Wiley  Structure 
Presentation transcript:

Structures of herbicides in complex with their detoxifying enzyme glutathione S- transferase – explanations for the selectivity of the enzyme in plants  Lars Prade, Robert Huber, Babara Bieseler  Structure  Volume 6, Issue 11, Pages 1445-1452 (November 1998) DOI: 10.1016/S0969-2126(98)00143-9

Figure 1 Chemical formulae for the herbicide–GSH complexes. (a) Atrazine, (b) FOE-4053, (c) alachlor and (d) metolachlor. SG represents the GSH moiety. Structure 1998 6, 1445-1452DOI: (10.1016/S0969-2126(98)00143-9)

Figure 2 Stereoview of the active site of GST-I from maize. The bound atrazine–GSH conjugate is shown in red. Residues of the H site are labelled; atoms are shown in standard colours. The final |2Fo–Fc| map contoured at 0.9σ is shown in blue and the |Fo–Fc| map, which was calculated before the inhibitor was build in, contoured at 2.5σ is shown in dark green. Structure 1998 6, 1445-1452DOI: (10.1016/S0969-2126(98)00143-9)

Figure 3 Stereoview of the active site of araGST in complex with the FOE-4053–GSH conjugate. The bound FOE-4053–GSH is shown in green. All residues contributing to the H site are labelled; atoms are shown in standard colours. The final |2Fo–Fc| map contoured at 0.9σ is shown in blue and the |Fo–Fc| map, which was calculated before the inhibitor was built in, contoured at 2.5σ is shown in red. Structure 1998 6, 1445-1452DOI: (10.1016/S0969-2126(98)00143-9)

Figure 4 Schematic drawings of the transition states and products of the snar and sn2 reactions. The important angles are marked and their values are given. The transition states of (a) the snar and (b) the sn2 reactions. (c,d) The products of these reactions. Structure 1998 6, 1445-1452DOI: (10.1016/S0969-2126(98)00143-9)

Figure 5 Overlay of the active sites of GST-I and araGST. The atrazine–GSH conjugate is shown in red and the FOE-4053–GSH conjugate is in green. Residues of the GST-I H site are in brown and those of araGST are in blue. The numbering is according to the GST-I sequence. Structure 1998 6, 1445-1452DOI: (10.1016/S0969-2126(98)00143-9)

Figure 6 Amino acid sequence alignment of five plant GST sequences. The sequences are labelled according to their name in the Swiss Prot database: GTH1_Wheat [38], GTH4_Maize [39], GTH1_Maize [19], GTH4_Arath [40] and GTH3_Maize [20]. The numbering is according to the GST-I sequence. Residues participating in the G and H sites are shown in green and red, respectively. Structure 1998 6, 1445-1452DOI: (10.1016/S0969-2126(98)00143-9)