4ea9

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4ea9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Caulobacter_vibrioides Caulobacter vibrioides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EA9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EA9 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4ea9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Caulobacter_vibrioides Caulobacter vibrioides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EA9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EA9 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=JBT:GDP-N-ACETYLPEROSAMINE-COENZYME+A'>JBT</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 0.9&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=JBT:GDP-N-ACETYLPEROSAMINE-COENZYME+A'>JBT</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=4ea9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ea9 OCA], [https://pdbe.org/4ea9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ea9 RCSB], [https://www.ebi.ac.uk/pdbsum/4ea9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ea9 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=4ea9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ea9 OCA], [https://pdbe.org/4ea9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ea9 RCSB], [https://www.ebi.ac.uk/pdbsum/4ea9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ea9 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/O85353_CAUVI O85353_CAUVI]]
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[https://www.uniprot.org/uniprot/O85353_CAUVI O85353_CAUVI]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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N-acetylperosamine is an unusual dideoxysugar found in the O-antigens of some Gram-negative bacteria including the pathogenic Escherichia coli strain O157:H7. The last step in its biosynthesis is catalyzed by PerB, an N-acetyltransferase belonging to the left-handed beta-helix superfamily of proteins. Here we describe a combined structural and functional investigation on PerB from Caulobacter crescentus. For this study, three structures were determined to 1.0 A resolution or better: the enzyme in complex with CoA and GDP-perosamine, the protein with bound CoA and GDP-N-acetylperosamine, and the enzyme containing a tetrahedral transition state mimic bound in the active site. Each subunit of the trimeric enzyme folds into two distinct regions. The N-terminal domain is globular and dominated by a six-stranded mainly parallel beta-sheet. It provides most of the interactions between the protein and GDP-perosamine. The C-terminal domain consists of a left-handed beta-helix, which has nearly seven turns. This region provides the scaffold for CoA binding. On the basis of these high-resolution structures, site-directed mutant proteins were constructed to test the roles of His 141 and Asp 142 in the catalytic mechanism. Kinetic data and pH rate profiles are indicative of His 141 serving as a general base. In addition, the backbone amide group of Gly 159 provides an oxyanion hole for stabilization of the tetrahedral transition state. The pH rate profiles are also consistent with the GDP-linked amino sugar substrate entering the active site in its unprotonated form. Finally, for this investigation, we show that PerB can accept GDP-3-deoxyperosamine as an alternative substrate, thus representing the production of a novel trideoxysugar.
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The Catalytic Mechanism of Perosamine N-Acetyltransferase Revealed by High Resolution X-ray Crystallographic Studies and Kinetic Analyses.,Thoden JB, Reinhardt LA, Cook PD, Menden P, Cleland WW, Holden HM Biochemistry. 2012 Mar 23. PMID:22443398<ref>PMID:22443398</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4ea9" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>

Current revision

X-ray structure of GDP-perosamine N-acetyltransferase in complex with transition state analog at 0.9 Angstrom resolution

PDB ID 4ea9

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