Solution and crystal structure of BA42, a protein from the Antarctic bacterium Bizionia argentinensis comprised of a stand-alone TPM domain

The structure of the BA42 protein belonging to the Antarctic flavobacterium Bizionia argentinensis was determined by nuclear magnetic resonance and X-ray crystallography. This is the first structure of a member of the PF04536 family comprised of a stand-alone TPM domain. The structure reveals a new...

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Detalles Bibliográficos
Autores principales: Aran, M., Smal, C., Pellizza, L., Gallo, M., Otero, L.H., Klinke, S., Goldbaum, F.A., Ithurralde, E.R., Bercovich, A., Mac Cormack, W.P., Turjanski, A.G., Cicero, D.O.
Formato: JOUR
Materias:
Antarctic bacteria
BA42
Bizionia argentinensis
Nuclear magnetic resonance
Protein structure
Structural genomics
X-ray crystallography
ba42 protein
bacterial protein
metal ion
unclassified drug
calcium
metal
Article
beta sheet
binding affinity
binding site
crystal structure
Flavobacterium
metal binding
molecular dynamics
nonhuman
nuclear magnetic resonance
priority journal
protein domain
protein family
protein stability
X ray crystallography
amino acid sequence
animal
Antarctica
chemical structure
chemistry
circular dichroism
Flavobacteriaceae
genetics
metabolism
molecular genetics
protein conformation
protein tertiary structure
sequence homology
Bacteria (microorganisms)
Bizionia
Amino Acid Sequence
Animals
Antarctic Regions
Bacterial Proteins
Binding Sites
Calcium
Circular Dichroism
Crystallography, X-Ray
Metals
Models, Molecular
Molecular Sequence Data
Nuclear Magnetic Resonance, Biomolecular
Protein Conformation
Protein Stability
Protein Structure, Tertiary
Sequence Homology, Amino Acid
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_08873585_v82_n11_p3062_Aran
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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