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4eab

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==X-ray crystal structure of the H141A mutant of GDP-perosamine N-acetyl transferase from Caulobacter crescentus in complex with CoA and GDP-perosamine==
==X-ray crystal structure of the H141A mutant of GDP-perosamine N-acetyl transferase from Caulobacter crescentus in complex with CoA and GDP-perosamine==
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<StructureSection load='4eab' size='340' side='right' caption='[[4eab]], [[Resolution|resolution]] 1.35&Aring;' scene=''>
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<StructureSection load='4eab' size='340' side='right'caption='[[4eab]], [[Resolution|resolution]] 1.35&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4eab]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Caulobacter_vibrioides Caulobacter vibrioides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EAB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EAB FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4eab]] 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=4EAB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EAB FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=JB2:GDP-PEROSAMINE'>JB2</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 1.35&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ea7|4ea7]], [[4ea8|4ea8]], [[4ea9|4ea9]], [[4eaa|4eaa]]</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=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=JB2:GDP-PEROSAMINE'>JB2</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CC_1011, wbqR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=155892 Caulobacter vibrioides])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4eab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eab OCA], [https://pdbe.org/4eab PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4eab RCSB], [https://www.ebi.ac.uk/pdbsum/4eab PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4eab ProSAT]</span></td></tr>
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<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=4eab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eab OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4eab RCSB], [http://www.ebi.ac.uk/pdbsum/4eab PDBsum]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/O85353_CAUVI O85353_CAUVI]
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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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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Caulobacter vibrioides]]
[[Category: Caulobacter vibrioides]]
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[[Category: Cleland, W W]]
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[[Category: Large Structures]]
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[[Category: Cook, P D]]
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[[Category: Cleland WW]]
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[[Category: Holden, H M]]
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[[Category: Cook PD]]
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[[Category: Menden, P]]
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[[Category: Holden HM]]
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[[Category: Reinhardt, L A]]
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[[Category: Menden P]]
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[[Category: Thoden, J B]]
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[[Category: Reinhardt LA]]
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[[Category: Acetyl coenzyme some]]
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[[Category: Thoden JB]]
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[[Category: Acetyltransferase]]
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[[Category: Beta helix]]
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[[Category: Gdp-perosamine]]
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[[Category: Transferase]]
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Current revision

X-ray crystal structure of the H141A mutant of GDP-perosamine N-acetyl transferase from Caulobacter crescentus in complex with CoA and GDP-perosamine

PDB ID 4eab

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