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A conserved fold for fimbrial components revealed by the crystal structure of a putative fimbrial assembly protein (BT1062) from Bacteroides thetaiotaomicron at 2.2 Å resolution
- Source :
- Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Acta crystallographica. Section F, Structural biology and crystallization communications, vol 66, iss Pt 10
- Publication Year :
- 2010
- Publisher :
- International Union of Crystallography, 2010.
-
Abstract
- The crystal structure of BT1062 from Bacteroides thetaiotaomicron revealed a conserved fold that is widely adopted by fimbrial components.<br />BT1062 from Bacteroides thetaiotaomicron is a homolog of Mfa2 (PGN0288 or PG0179), which is a component of the minor fimbriae in Porphyromonas gingivalis. The crystal structure of BT1062 revealed a conserved fold that is widely adopted by fimbrial components.
- Subjects :
- Models, Molecular
Protein Folding
Fimbria
Crystallography, X-Ray
Biochemistry
fimbriae
Pilus
Fimbriae Proteins
fluids and secretions
Structural Biology
Models
Bacteroides
Peptide sequence
0303 health sciences
Crystallography
biology
Human Gut Microbiome
Bacterial
food and beverages
Biological Sciences
Condensed Matter Physics
pili
PG0179
Bacteroides thetaiotaomicron
Protein Structure
DUF1812
Mfa2
Molecular Sequence Data
Biophysics
Sequence alignment
digestive system
Fimbriae
03 medical and health sciences
Genetics
Amino Acid Sequence
BT1062
Porphyromonas gingivalis
PGN0288
030304 developmental biology
Structural Homology
030306 microbiology
Protein
Molecular
biochemical phenomena, metabolism, and nutrition
biology.organism_classification
bacterial infections and mycoses
Protein Structure, Tertiary
carbohydrates (lipids)
Structural Homology, Protein
Fimbriae, Bacterial
Chemical Sciences
X-Ray
bacteria
PF08842
Digestive Diseases
Sequence Alignment
Tertiary
Subjects
Details
- Language :
- English
- ISSN :
- 17443091
- Volume :
- 66
- Issue :
- Pt 10
- Database :
- OpenAIRE
- Journal :
- Acta Crystallographica Section F: Structural Biology and Crystallization Communications
- Accession number :
- edsair.doi.dedup.....007ddefbe60d7894f526bbc973ac2fbb