NMR assignment of the Rhodobacter sphaeroides fasciclin-1 domain protein (Fdp).
We report the almost complete assignment of 1H, 13C and 15N nuclei in the 137-residue his-tagged fasciclin domain protein (Fdp) from Rhodobacter sphaeroides. Fdp is homologous to fasciclin I domains, including Drosophila FAS1 and M. tuberculosis MPB70 and plays a role in cell adhesion.
Moody
Robert G
RG
Astbury Centre for Structural Molecular Biology, Institute for Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, UK.
Phillips-Jones
Mary K
MK
Williamson
Mike P
MP
D000818:Animals; D001422:Bacterial Adhesion; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D015816:Cell Adhesion Molecules, Neuronal / Q000737:chemistry* / Q000235:genetics; D029721:Drosophila Proteins / Q000737:chemistry; D005798:Genes, Bacterial; D009169:Mycobacterium tuberculosis / Q000737:chemistry; D019906:Nuclear Magnetic Resonance, Biomolecular; D017434:Protein Structure, Tertiary; D012242:Rhodobacter sphaeroides / Q000737:chemistry* / Q000235:genetics
D001426:Bacterial Proteins; D015816:Cell Adhesion Molecules, Neuronal; D029721:Drosophila Proteins; C051641:fasciclin I