Structure of the haem-chaperone Proteobacteria-protein HemS

An Induced Fit Conformational Change Underlies the Binding Mechanism of the Heme Transport Proteobacteria-Protein Hems.

Crystallization and Preliminary X-Ray Diffraction Analysis of the Haem-Binding Protein Hems from Yersinia Enterocolitica.

MSKSIYEQYLQAKADNPGKYARDLATLMGISEAELTHSRVSHDAKRLKGDARALLAALEAVGEVKAITRNTYAVHEQMGR
YENQHLNGHAGLILNPRNLDLRLFLNQWASAFTLTEETRHGVRHSIQFFDHQGDALHKVYVTEQTDMPAWEALLAQFITT
ENPELQLEPLSAPEVTEPTATDEAVDAEWRAMTDVHEFFQLLKRNNLTRQQAFRAVGNDLAYQVDNSSLTQLLNIAQQEQ
NEIMIFVGNRGCVQIFTGMIEKVTPHQDWINVFNQRFTLHLIETTIAESWITRKPTKDGFVTSLELFAADGTQIAQLYGQ
RTEGQPEQTQWRDQIARLNNKDIAA

50MM TRIS-HCL PH8.5, 1.8M AMMONIUM SULPHATE, 4% PEG400

STRUCTURE OF THE HAEM-CHAPERONE PROTEOBACTERIA -PROTEIN HEMS

ASN 162 IS ILE IN THE SEQUENCE FILE P31517. COMPARISON OF MULTIPLE SEQUENCE ALIGNMENTS OF HEMS HOMOLOGUES AND HEMS FROM Y.ENTEROCOLITICA STRAIN 8081 SEQUENCED AT THE SANGER INSTITUTE, SHOW ASN AT THIS POSITION.

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. RESIDUES 1-3, 170-179 AND 342-345 ARE DISORDERED. NE2 OF HIS196 IS COORDINATING THE HAEM-IRON.

TRANSPORT PROTEIN, CONFORMATIONAL CHANGES, HAEM, IRON, TRANSPORT, ION TRANSPORT, PROTEOBACTERIA, IRON TRANSPORT, HAEM-BINDING PROTEIN