7ck1

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==Crystal structure of arabidopsis CESA3 catalytic domain==
==Crystal structure of arabidopsis CESA3 catalytic domain==
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<StructureSection load='7ck1' size='340' side='right'caption='[[7ck1]]' scene=''>
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<StructureSection load='7ck1' size='340' side='right'caption='[[7ck1]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CK1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CK1 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[7ck1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CK1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CK1 FirstGlance]. <br>
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</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=7ck1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ck1 OCA], [https://pdbe.org/7ck1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ck1 RCSB], [https://www.ebi.ac.uk/pdbsum/7ck1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ck1 ProSAT]</span></td></tr>
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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=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CESA3, ATHB, CEV1, ELI1, IXR1, RSW5, At5g05170, K2A11.4 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</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=7ck1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ck1 OCA], [https://pdbe.org/7ck1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ck1 RCSB], [https://www.ebi.ac.uk/pdbsum/7ck1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ck1 ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[[https://www.uniprot.org/uniprot/CESA3_ARATH CESA3_ARATH]] Catalytic subunit of cellulose synthase terminal complexes ('rosettes'), required for beta-1,4-glucan microfibril crystallization, a major mechanism of the cell wall formation. Involved in the primary cell wall formation, especially in roots.<ref>PMID:11340179</ref> <ref>PMID:12068120</ref> <ref>PMID:12119374</ref> <ref>PMID:12713541</ref> <ref>PMID:17878302</ref> <ref>PMID:17878303</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Cellulose is synthesized by cellulose synthases (CESAs) from the glycosyltransferase GT-2 family. In plants, the CESAs form a six-lobed rosette-shaped CESA complex (CSC). Here we report crystal structures of the catalytic domain of Arabidopsis thaliana CESA3 (AtCESA3(CatD)) in both apo and uridine diphosphate (UDP)-glucose (UDP-Glc)-bound forms. AtCESA3(CatD) has an overall GT-A fold core domain sandwiched between a plant-conserved region (P-CR) and a class-specific region (C-SR). By superimposing the structure of AtCESA3(CatD) onto the bacterial cellulose synthase BcsA, we found that the coordination of the UDP-Glc differs, indicating different substrate coordination during cellulose synthesis in plants and bacteria. Moreover, structural analyses revealed that AtCESA3(CatD) can form a homodimer mainly via interactions between specific beta strands. We confirmed the importance of specific amino acids on these strands for homodimerization through yeast and in planta assays using point-mutated full-length AtCESA3. Our work provides molecular insights into how the substrate UDP-Glc is coordinated in the CESAs and how the CESAs might dimerize to eventually assemble into CSCs in plants.
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Structure of Arabidopsis CESA3 catalytic domain with its substrate UDP-glucose provides insight into the mechanism of cellulose synthesis.,Qiao Z, Lampugnani ER, Yan XF, Khan GA, Saw WG, Hannah P, Qian F, Calabria J, Miao Y, Gruber G, Persson S, Gao YG Proc Natl Acad Sci U S A. 2021 Mar 16;118(11). pii: 2024015118. doi:, 10.1073/pnas.2024015118. PMID:33729990<ref>PMID:33729990</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 7ck1" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Arath]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Gao YG]]
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[[Category: Gao, Y G]]
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[[Category: Qiao Z]]
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[[Category: Qiao, Z]]
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[[Category: Enzyme]]
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[[Category: Plant protein]]
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[[Category: Synthase]]

Revision as of 10:47, 31 March 2021

Crystal structure of arabidopsis CESA3 catalytic domain

PDB ID 7ck1

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