Evidence for an elongated dimeric structure of heparin-binding hemagglutinin from Mycobacterium tuberculosis.
Heparin-binding hemagglutinin (HBHA) is a virulence factor of tuberculosis which is responsible for extrapulmonary dissemination of this disease. A thorough biochemical characterization of HBHA has provided experimental evidence of a coiled-coil nature of HBHA. These data, together with the low-resolution structures of a full-length form and a truncated form of HBHA obtained by small-angle X-ray scattering, have unambiguously indicated that HBHA has a dimeric structure with an elongated shape.
Esposito
Carla
C
Istituto di Biostrutture e Bioimmagini, C.N.R., I-80134, Napoli, Italy.
Pethoukov
Maxim V
MV
Svergun
Dmitri I
DI
Ruggiero
Alessia
A
Pedone
Carlo
C
Pedone
Emilia
E
Berisio
Rita
R
D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D002942:Circular Dichroism; D019281:Dimerization; D037102:Lectins / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D009169:Mycobacterium tuberculosis / Q000378:metabolism*; D012542:Scattering, Radiation; D017356:Synchrotrons; D014965:X-Rays
D001426:Bacterial Proteins; D037102:Lectins; C104578:heparin-binding hemagglutinin