ArticleActa crystallographica. Section F, Structural biology and crystallization communications2010
Structure of BT_3984, a member of the SusD/RagB family of nutrient-binding molecules.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed, 13 citations in OpenAlex.
- Metagenome-derived SusD-homologs affiliated with Bacteroidota bind to synthetic polymers.Applied and environmental microbiology · 2024Article
- Cell Surface Xyloglucan Recognition and Hydrolysis by the Human Gut Commensal Bacteroides uniformis.Applied and environmental microbiology · 2022Review
- Comparison of Alginate Utilization Pathways in Culturable Bacteria Isolated From Arctic and Antarctic Marine Environments.Frontiers in microbiology · 2021Article
- Initial Mapping of the New York City Wastewater Virome.mSystems · 2020Article
- Polysaccharide Utilization Loci: Fueling Microbial Communities.Journal of bacteriology · 2017Review
- Structure of RagB, a major immunodominant outer-membrane surface receptor antigen of Porphyromonas gingivalis.Molecular oral microbiology · 2016Article
- Molecular characterization of novel pyridoxal-5'-phosphate-dependent enzymes from the human microbiome.Protein science : a publication of the Protein Society · 2014Article
Corrections and comments
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Authors and funding
47 authors at 7 institutions in 1 country.
Funding
Abstract
The crystal structure of the Bacteroides thetaiotaomicron protein BT_3984 was determined to a resolution of 1.7 Å and was the first structure to be determined from the extensive SusD family of polysaccharide-binding proteins. SusD is an essential component of the sus operon that defines the paradigm for glycan utilization in dominant members of the human gut microbiota. Structural analysis of BT_3984 revealed an N-terminal region containing several tetratricopeptide repeats (TPRs), while the signature C-terminal region is less structured and contains extensive loop regions. Sequence and structure analysis of BT_3984 suggests the presence of binding interfaces for other proteins from the polysaccharide-utilization complex.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.