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2jdd

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Glyphosate N-acetyltransferase bound to acetyl COA and 3-phosphoglycerate

Structural highlights

2jdd is a 1 chain structure with sequence from Bacillus licheniformis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.6Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q65LG7_BACLD

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

GAT is an N-acetyltransferase from Bacillus licheniformis that was optimized by gene shuffling for acetylation of the broad spectrum herbicide, glyphosate, forming the basis of a novel mechanism of glyphosate tolerance in transgenic plants (Castle, L. A., Siehl, D. L., Gorton, R., Patten, P. A., Chen, Y. H., Bertain, S., Cho, H. J., Duck, N., Wong, J., Liu, D., and Lassner, M. W. (2004) Science 304, 1151-1154). The 1.6-A resolution crystal structure of an optimized GAT variant in ternary complex with acetyl coenzyme A and a competitive inhibitor, 3-phosphoglyerate, defines GAT as a member of the GCN5-related family of N-acetyltransferases. Four active site residues (Arg-21, Arg-73, Arg-111, and His-138) contribute to a positively charged substrate-binding site that is conserved throughout the GAT subfamily. Structural and kinetic data suggest that His-138 functions as a catalytic base via substrate-assisted deprotonation of the glyphosate secondary amine, whereas another active site residue, Tyr-118, functions as a general acid. Although the physiological substrate is unknown, native GAT acetylates D-2-amino-3-phosphonopropionic acid with a kcat/Km of 1500 min-1 mM-1. Kinetic data show preferential binding of short analogs to native GAT and progressively better binding of longer analogs to optimized variants. Despite a 200-fold increase in kcat and a 5.4-fold decrease in Km for glyphosate, only 4 of the 21 substitutions present in R7 GAT lie in the active site. Single-site revertants constructed at these positions suggest that glyphosate binding is optimized through substitutions that increase the size of the substrate-binding site. The large improvement in kcat is likely because of the cooperative effects of additional substitutions located distal to the active site.

The molecular basis of glyphosate resistance by an optimized microbial acetyltransferase.,Siehl DL, Castle LA, Gorton R, Keenan RJ J Biol Chem. 2007 Apr 13;282(15):11446-55. Epub 2007 Feb 1. PMID:17272278^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Siehl DL, Castle LA, Gorton R, Keenan RJ. The molecular basis of glyphosate resistance by an optimized microbial acetyltransferase. J Biol Chem. 2007 Apr 13;282(15):11446-55. Epub 2007 Feb 1. PMID:17272278 doi:10.1074/jbc.M610267200

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2jdd"

@@ Line 3: / Line 3: @@
 <StructureSection load='2jdd' size='340' side='right'caption='[[2jdd]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2jdd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"clostridium_licheniforme"_weigmann_1898 "clostridium licheniforme" weigmann 1898]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JDD OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2JDD FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2jdd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JDD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JDD FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3PG:3-PHOSPHOGLYCERIC+ACID'>3PG</scene>, <scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2jdd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jdd OCA], [http://pdbe.org/2jdd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2jdd RCSB], [http://www.ebi.ac.uk/pdbsum/2jdd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2jdd ProSAT]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3PG:3-PHOSPHOGLYCERIC+ACID'>3PG</scene>, <scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2jdd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jdd OCA], [https://pdbe.org/2jdd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jdd RCSB], [https://www.ebi.ac.uk/pdbsum/2jdd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jdd ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q65LG7_BACLD Q65LG7_BACLD]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 30: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Clostridium licheniforme weigmann 1898]]
+[[Category: Bacillus licheniformis]]
 [[Category: Large Structures]]
-[[Category: Castle, L A]]
+[[Category: Castle LA]]
-[[Category: Gorton, R]]
+[[Category: Gorton R]]
-[[Category: Keenan, R J]]
+[[Category: Keenan RJ]]
-[[Category: Siehl, D L]]
+[[Category: Siehl DL]]
-[[Category: Glyphosate]]
-[[Category: Gnat]]
-[[Category: N-acetyltransferase]]
-[[Category: Transferase]]

2jdd

From Proteopedia

Current revision

Glyphosate N-acetyltransferase bound to acetyl COA and 3-phosphoglycerate

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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