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6cci
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | The | + | ==The Crystal Structure of XOAT1== |
| + | <StructureSection load='6cci' size='340' side='right'caption='[[6cci]], [[Resolution|resolution]] 1.85Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6cci]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CCI OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6CCI FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ESK1, TBL29, At3g55990, F27K19.170 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</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=6cci FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cci OCA], [http://pdbe.org/6cci PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cci RCSB], [http://www.ebi.ac.uk/pdbsum/6cci PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cci ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/TBL29_ARATH TBL29_ARATH]] Probable xylan acetyltransferase required for 2-O- and 3-O-monoacetylation of xylosyl residues in xylan. Negative regulator of cold acclimation. Involved in water economy as well as salt tolerance. Regulated at the transcriptional level by NAC012/SND1 (PubMed:17316173, PubMed:19054354, PubMed:19061521, PubMed:21408051, PubMed:23340742, PubMed:23659919). May act as a bridging protein that binds pectin and other cell wall polysaccharides. Probably involved in maintaining esterification of pectins (By similarity).[UniProtKB:Q9FG35]<ref>PMID:17316173</ref> <ref>PMID:19054354</ref> <ref>PMID:19061521</ref> <ref>PMID:21408051</ref> <ref>PMID:23340742</ref> <ref>PMID:23659919</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Xylans are a major component of plant cell walls. O-Acetyl moieties are the dominant backbone substituents of glucuronoxylan in dicots and play a major role in the polymer-polymer interactions that are crucial for wall architecture and normal plant development. Here, we describe the biochemical, structural, and mechanistic characterization of Arabidopsis (Arabidopsis thaliana) xylan O-acetyltransferase 1 (XOAT1), a member of the plant-specific Trichome Birefringence Like (TBL) family. Detailed characterization of XOAT1-catalyzed reactions by real-time NMR confirms that it exclusively catalyzes the 2-O-acetylation of xylan, followed by nonenzymatic acetyl migration to the O-3 position, resulting in products that are monoacetylated at both O-2 and O-3 positions. In addition, we report the crystal structure of the catalytic domain of XOAT1, which adopts a unique conformation that bears some similarities to the alpha/beta/alpha topology of members of the GDSL-like lipase/acylhydrolase family. Finally, we use a combination of biochemical analyses, mutagenesis, and molecular simulations to show that XOAT1 catalyzes xylan acetylation through formation of an acyl-enzyme intermediate, Ac-Ser-216, by a double displacement bi-bi mechanism involving a Ser-His-Asp catalytic triad and unconventionally uses an Arg residue in the formation of an oxyanion hole. | ||
| - | + | Molecular Mechanism of Polysaccharide Acetylation by the Arabidopsis Xylan O-acetyltransferase XOAT1.,Lunin VV, Wang HT, Bharadwaj VS, Alahuhta M, Pena MJ, Yang JY, Archer-Hartmann SA, Azadi P, Himmel ME, Moremen KW, York WS, Bomble YJ, Urbanowicz BR Plant Cell. 2020 Jul;32(7):2367-2382. doi: 10.1105/tpc.20.00028. Epub 2020 Apr, 30. PMID:32354790<ref>PMID:32354790</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Alahuhta, P | + | <div class="pdbe-citations 6cci" style="background-color:#fffaf0;"></div> |
| - | [[Category: Lunin, V | + | |
| + | ==See Also== | ||
| + | *[[Theoretical models|Theoretical models]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Arath]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Alahuhta, P M]] | ||
| + | [[Category: Lunin, V V]] | ||
| + | [[Category: Acetyltransferase]] | ||
| + | [[Category: Arabidopsis thaliana]] | ||
| + | [[Category: Transferase]] | ||
Current revision
The Crystal Structure of XOAT1
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