Architecture of a catalytically active homotrimeric plant cellulose synthase complex.
Identifieur interne : 000560 ( Main/Exploration ); précédent : 000559; suivant : 000561Architecture of a catalytically active homotrimeric plant cellulose synthase complex.
Auteurs : Pallinti Purushotham [États-Unis] ; Ruoya Ho [États-Unis] ; Jochen Zimmer [États-Unis]Source :
- Science (New York, N.Y.) [ 1095-9203 ] ; 2020.
Descripteurs français
- KwdFr :
- MESH :
- composition chimique : Complexes multienzymatiques, Glucosyltransferases, Protéines végétales.
- enzymologie : Populus.
- Biocatalyse, Domaine catalytique, Multimérisation de protéines.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Glucosyltransferases, Multienzyme Complexes, Plant Proteins.
- enzymology : Populus.
- Biocatalysis, Catalytic Domain, Protein Multimerization.
Abstract
Cellulose is an essential plant cell wall component and represents the most abundant biopolymer on Earth. Supramolecular plant cellulose synthase complexes organize multiple linear glucose polymers into microfibrils as load-bearing wall components. We determined the structure of a poplar cellulose synthase CesA homotrimer that suggests a molecular basis for cellulose microfibril formation. This complex, stabilized by cytosolic plant-conserved regions and helical exchange within the transmembrane segments, forms three channels occupied by nascent cellulose polymers. Secretion steers the polymers toward a common exit point, which could facilitate protofibril formation. CesA's N-terminal domains assemble into a cytosolic stalk that interacts with a microtubule-tethering protein and may thus be involved in CesA localization. Our data suggest how cellulose synthase complexes assemble and provide the molecular basis for plant cell wall engineering.
DOI: 10.1126/science.abb2978
PubMed: 32646917
Affiliations:
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Supramolecular plant cellulose synthase complexes organize multiple linear glucose polymers into microfibrils as load-bearing wall components. We determined the structure of a poplar cellulose synthase CesA homotrimer that suggests a molecular basis for cellulose microfibril formation. This complex, stabilized by cytosolic plant-conserved regions and helical exchange within the transmembrane segments, forms three channels occupied by nascent cellulose polymers. Secretion steers the polymers toward a common exit point, which could facilitate protofibril formation. CesA's N-terminal domains assemble into a cytosolic stalk that interacts with a microtubule-tethering protein and may thus be involved in CesA localization. Our data suggest how cellulose synthase complexes assemble and provide the molecular basis for plant cell wall engineering.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">32646917</PMID><DateCompleted><Year>2020</Year><Month>09</Month><Day>25</Day></DateCompleted><DateRevised><Year>2020</Year><Month>09</Month><Day>25</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1095-9203</ISSN><JournalIssue CitedMedium="Internet"><Volume>369</Volume><Issue>6507</Issue><PubDate><Year>2020</Year><Month>08</Month><Day>28</Day></PubDate></JournalIssue><Title>Science (New York, N.Y.)</Title><ISOAbbreviation>Science</ISOAbbreviation></Journal><ArticleTitle>Architecture of a catalytically active homotrimeric plant cellulose synthase complex.</ArticleTitle><Pagination><MedlinePgn>1089-1094</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1126/science.abb2978</ELocationID><Abstract><AbstractText>Cellulose is an essential plant cell wall component and represents the most abundant biopolymer on Earth. Supramolecular plant cellulose synthase complexes organize multiple linear glucose polymers into microfibrils as load-bearing wall components. We determined the structure of a poplar cellulose synthase CesA homotrimer that suggests a molecular basis for cellulose microfibril formation. This complex, stabilized by cytosolic plant-conserved regions and helical exchange within the transmembrane segments, forms three channels occupied by nascent cellulose polymers. Secretion steers the polymers toward a common exit point, which could facilitate protofibril formation. CesA's N-terminal domains assemble into a cytosolic stalk that interacts with a microtubule-tethering protein and may thus be involved in CesA localization. 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