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4mzu

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==Crystal structure of FdtD, a bifunctional ketoisomerase/N-acetyltransferase from Shewanella denitrificans==
==Crystal structure of FdtD, a bifunctional ketoisomerase/N-acetyltransferase from Shewanella denitrificans==
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<StructureSection load='4mzu' size='340' side='right' caption='[[4mzu]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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<StructureSection load='4mzu' size='340' side='right'caption='[[4mzu]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4mzu]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Shedo Shedo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MZU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MZU FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4mzu]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Shewanella_denitrificans_OS217 Shewanella denitrificans OS217]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MZU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MZU 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=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TDR:THYMINE'>TDR</scene>, <scene name='pdbligand=TYD:THYMIDINE-5-DIPHOSPHATE'>TYD</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]] 2.2&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FdtD, Sden_2659 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=318161 SHEDO])</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=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TDR:THYMINE'>TDR</scene>, <scene name='pdbligand=TYD:THYMIDINE-5-DIPHOSPHATE'>TYD</scene></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=4mzu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mzu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4mzu RCSB], [http://www.ebi.ac.uk/pdbsum/4mzu PDBsum]</span></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=4mzu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mzu OCA], [https://pdbe.org/4mzu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mzu RCSB], [https://www.ebi.ac.uk/pdbsum/4mzu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mzu ProSAT]</span></td></tr>
</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/Q12KT8_SHEDO Q12KT8_SHEDO]
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Unusual N-acetylated sugars have been observed on the O-antigens of some Gram-negative bacteria and on the S-layers of both Gram-positive and Gram-negative bacteria. One such sugar is 3-acetamido-3,6-dideoxy-alpha-d-galactose or Fuc3NAc. The pathway for its production requires five enzymes with the first step involving the attachment of dTMP to glucose-1-phosphate. Here, we report a structural and biochemical characterization of a bifunctional enzyme from Shewanella denitificans thought to be involved in the biosynthesis of dTDP-Fuc3NAc. On the basis of a bioinformatics analysis, the enzyme, hereafter referred to as FdtD, has been postulated to catalyze the third and fifth steps in the pathway, namely, a 3,4-keto isomerization and an N-acetyltransferase reaction. For the X-ray analysis reported here, the enzyme was crystallized in the presence of dTDP and CoA. The crystal structure shows that FdtD adopts a hexameric quaternary structure with 322 symmetry. Each subunit of the hexamer folds into two distinct domains connected by a flexible loop. The N-terminal domain adopts a left-handed beta-helix motif and is responsible for the N-acetylation reaction. The C-terminal domain folds into an antiparallel flattened beta-barrel that harbors the active site responsible for the isomerization reaction. Biochemical assays verify the two proposed catalytic activities of the enzyme and reveal that the 3,4-keto isomerization event leads to the inversion of configuration about the hexose C-4' carbon.
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Structural and Biochemical Characterization of a Bifunctional Ketoisomerase/N-Acetyltransferase from Shewanella denitrificans.,Chantigian DP, Thoden JB, Holden HM Biochemistry. 2013 Nov 19;52(46):8374-85. doi: 10.1021/bi401170t. Epub 2013 Nov, 4. PMID:24128043<ref>PMID:24128043</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>
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[[Category: Shedo]]
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[[Category: Large Structures]]
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[[Category: Chantigian, D P]]
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[[Category: Shewanella denitrificans OS217]]
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[[Category: Holden, H M]]
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[[Category: Chantigian DP]]
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[[Category: Thoden, J B]]
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[[Category: Holden HM]]
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[[Category: Acetyl-coenzyme some]]
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[[Category: Thoden JB]]
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[[Category: Beta-helix]]
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[[Category: Cupin]]
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[[Category: Dtdp-4-keto-6-deoxyglucose]]
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[[Category: Dtdp-fuc3n]]
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[[Category: Isomerase]]
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[[Category: Ketoisomerase]]
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[[Category: N-acetyltransferase]]
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[[Category: Transferase]]
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Current revision

Crystal structure of FdtD, a bifunctional ketoisomerase/N-acetyltransferase from Shewanella denitrificans

PDB ID 4mzu

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