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7ck2

From Proteopedia

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Current revision

Crystal structure of Arabidopsis CESA3 catalytic domain with UDP-Glucose

Structural highlights

7ck2 is a 2 chain structure with sequence from Arath. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Gene:	CESA3, ATHB, CEV1, ELI1, IXR1, RSW5, At5g05170, K2A11.4 (ARATH)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1] ^[2] ^[3] ^[4] ^[5] ^[6]

Publication Abstract from PubMed

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.

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^[7]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Ellis C, Turner JG. The Arabidopsis mutant cev1 has constitutively active jasmonate and ethylene signal pathways and enhanced resistance to pathogens. Plant Cell. 2001 May;13(5):1025-33. PMID:11340179
↑ Burn JE, Hocart CH, Birch RJ, Cork AC, Williamson RE. Functional analysis of the cellulose synthase genes CesA1, CesA2, and CesA3 in Arabidopsis. Plant Physiol. 2002 Jun;129(2):797-807. PMID:12068120 doi:http://dx.doi.org/10.1104/pp.010931
↑ Ellis C, Karafyllidis I, Wasternack C, Turner JG. The Arabidopsis mutant cev1 links cell wall signaling to jasmonate and ethylene responses. Plant Cell. 2002 Jul;14(7):1557-66. doi: 10.1105/tpc.002022. PMID:12119374 doi:http://dx.doi.org/10.1105/tpc.002022
↑ Cano-Delgado A, Penfield S, Smith C, Catley M, Bevan M. Reduced cellulose synthesis invokes lignification and defense responses in Arabidopsis thaliana. Plant J. 2003 May;34(3):351-62. doi: 10.1046/j.1365-313x.2003.01729.x. PMID:12713541 doi:http://dx.doi.org/10.1046/j.1365-313x.2003.01729.x
↑ Persson S, Paredez A, Carroll A, Palsdottir H, Doblin M, Poindexter P, Khitrov N, Auer M, Somerville CR. Genetic evidence for three unique components in primary cell-wall cellulose synthase complexes in Arabidopsis. Proc Natl Acad Sci U S A. 2007 Sep 25;104(39):15566-71. doi:, 10.1073/pnas.0706592104. Epub 2007 Sep 18. PMID:17878302 doi:http://dx.doi.org/10.1073/pnas.0706592104
↑ Desprez T, Juraniec M, Crowell EF, Jouy H, Pochylova Z, Parcy F, Hofte H, Gonneau M, Vernhettes S. Organization of cellulose synthase complexes involved in primary cell wall synthesis in Arabidopsis thaliana. Proc Natl Acad Sci U S A. 2007 Sep 25;104(39):15572-7. Epub 2007 Sep 18. PMID:17878303 doi:http://dx.doi.org/0706569104
↑ Qiao Z, Lampugnani ER, Yan XF, Khan GA, Saw WG, Hannah P, Qian F, Calabria J, Miao Y, Gruber G, Persson S, Gao YG. Structure of Arabidopsis CESA3 catalytic domain with its substrate UDP-glucose provides insight into the mechanism of cellulose synthesis. Proc Natl Acad Sci U S A. 2021 Mar 16;118(11). pii: 2024015118. doi:, 10.1073/pnas.2024015118. PMID:33729990 doi:http://dx.doi.org/10.1073/pnas.2024015118

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/7ck2"

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 7ck2 is ON HOLD
+==Crystal structure of Arabidopsis CESA3 catalytic domain with UDP-Glucose==
+<StructureSection load='7ck2' size='340' side='right'caption='[[7ck2]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[7ck2]] 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=7CK2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CK2 FirstGlance]. <br>
+</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>, <scene name='pdbligand=UPG:URIDINE-5-DIPHOSPHATE-GLUCOSE'>UPG</scene></td></tr>
+<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>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7ck2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ck2 OCA], [https://pdbe.org/7ck2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ck2 RCSB], [https://www.ebi.ac.uk/pdbsum/7ck2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ck2 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[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>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-Authors:
+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>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 7ck2" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Arath]]
+[[Category: Large Structures]]
+[[Category: Gao, Y G]]
+[[Category: Qiao, Z]]
+[[Category: Enzyme]]
+[[Category: Plant protein]]
+[[Category: Synthase]]

7ck2

From Proteopedia

Current revision

Crystal structure of Arabidopsis CESA3 catalytic domain with UDP-Glucose

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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