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PXD032013

PXD032013 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleSas20 is a highly flexible starch-binding protein in the Ruminococcus bromii cell-surface amylosome
DescriptionRuminococcus bromii is a keystone species in the human gut that has the rare ability to degrade dietary resistant starch (RS). This bacterium secretes a suite of starch-active proteins that work together within larger complexes called amylosomes that allow R. bromii to adhere to and degrade RS. Sas20 is one of the more abundant proteins assembled within amylosomes, but little could be predicted about its molecular features based upon amino acid sequence. Here, we perform a structure-function analysis of Sas20 which features two discrete starch-binding domains separated by a flexible linker. Sas20 domain 1 has an N-terminal β-sandwich followed by a cluster of α-helices and captures the non-reducing end of maltooligosaccharides between these structural features. The crystal structure of a close homolog of Sas20 domain 2 revealed a unique bilobed starch-binding groove that targets the helical 1,4-linked glycan chains found in amorphous regions of amylopectin and crystalline regions of amylose within starch granules. Affinity PAGE and isothermal titration calorimetry demonstrate both domains bind maltoheptaose and soluble starch with relatively high affinity (Kd  20 M) but exhibit limited or no binding to cyclodextrins. Small angle x-ray scattering analysis of the individual and combined domains support that these structures are highly flexible, which may allow the protein to adopt conformations that enhance its starch-targeting efficiency.
HostingRepositoryPRIDE
AnnounceDate2022-06-09
AnnouncementXMLSubmission_2022-06-09_02:03:09.953.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterFilipe Cerqueira
SpeciesList scientific name: Ruminococcus bromii L2-63; NCBI TaxID: 657321;
ModificationListmonohydroxylated residue; iodoacetamide derivatized residue; deamidated residue
InstrumentOrbitrap Fusion
Dataset History
RevisionDatetimeStatusChangeLog Entry
02022-03-02 09:52:28ID requested
12022-06-09 02:03:10announced
Publication List
Cerqueira FM, Photenhauer AL, Doden HL, Brown AN, Abdel-Hamid AM, Mora, ï, s S, Bayer EA, Wawrzak Z, Cann I, Ridlon JM, Hopkins JB, Koropatkin NM, Sas20 is a highly flexible starch-binding protein in the Ruminococcus bromii cell-surface amylosome. J Biol Chem, 298(5):101896(2022) [pubmed]
Keyword List
submitter keyword: R. bromii
Contact List
Nicole Koropatkin
contact affiliationUniversity of Michigan
contact emailnkoropat@umich.edu
lab head
Filipe Cerqueira
contact affiliationUniversity of Michigan
contact emailfilipehu@umich.edu
dataset submitter
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