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1ghe

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Revision as of 11:23, 28 July 2021

CRYSTAL STRUCTURE OF TABTOXIN RESISTANCE PROTEIN COMPLEXED WITH AN ACYL COENZYME A

Structural highlights

1ghe is a 2 chain structure with sequence from Pseaj. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[TTR_PSESZ] Renders tabtoxin-producing pathogens tolerant to their own phytotoxins.

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

Tabtoxin resistance protein (TTR) is an enzyme that renders tabtoxin-producing pathogens, such as Pseudomonas syringae, tolerant to their own phytotoxins. Here, we report the crystal structure of TTR complexed with its natural cofactor, acetyl coenzyme A (AcCoA), to 1.55A resolution. The binary complex forms a characteristic "V" shape for substrate binding and contains the four motifs conserved in the GCN5-related N-acetyltransferase (GNAT) superfamily, which also includes the histone acetyltransferases (HATs). A single-step mechanism is proposed to explain the function of three conserved residues, Glu92, Asp130 and Tyr141, in catalyzing the acetyl group transfer to its substrate. We also report that TTR possesses HAT activity and suggest an evolutionary relationship between TTR and other GNAT members.

Crystal structure of tabtoxin resistance protein complexed with acetyl coenzyme A reveals the mechanism for beta-lactam acetylation.,He H, Ding Y, Bartlam M, Sun F, Le Y, Qin X, Tang H, Zhang R, Joachimiak A, Liu J, Zhao N, Rao Z J Mol Biol. 2003 Jan 31;325(5):1019-30. PMID:12527305^[1]

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

References

↑ He H, Ding Y, Bartlam M, Sun F, Le Y, Qin X, Tang H, Zhang R, Joachimiak A, Liu J, Zhao N, Rao Z. Crystal structure of tabtoxin resistance protein complexed with acetyl coenzyme A reveals the mechanism for beta-lactam acetylation. J Mol Biol. 2003 Jan 31;325(5):1019-30. PMID:12527305

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/1ghe"

@@ Line 3: / Line 3: @@
 <StructureSection load='1ghe' size='340' side='right'caption='[[1ghe]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1ghe]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseaj Pseaj]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GHE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GHE FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1ghe]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseaj Pseaj]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GHE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GHE FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene></td></tr>
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ghe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ghe OCA], [http://pdbe.org/1ghe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ghe RCSB], [http://www.ebi.ac.uk/pdbsum/1ghe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ghe ProSAT]</span></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=1ghe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ghe OCA], [https://pdbe.org/1ghe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ghe RCSB], [https://www.ebi.ac.uk/pdbsum/1ghe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ghe ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/TTR_PSESZ TTR_PSESZ]] Renders tabtoxin-producing pathogens tolerant to their own phytotoxins.
+[[https://www.uniprot.org/uniprot/TTR_PSESZ TTR_PSESZ]] Renders tabtoxin-producing pathogens tolerant to their own phytotoxins.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1ghe

From Proteopedia

Revision as of 11:23, 28 July 2021

CRYSTAL STRUCTURE OF TABTOXIN RESISTANCE PROTEIN COMPLEXED WITH AN ACYL COENZYME A

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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