Polyvalent display of heme on hepatitis B virus capsid protein through coordination to hexahistidine tags.
The addition of a hexahistidine tag to the N terminus of the hepatitis B capsid protein gives rise to a self-assembled particle with 80 sites of high local density of histidine side chains. Iron protoporphyrin IX has been found to bind tightly at each of these sites, making a polyvalent system of well-defined spacing between metalloporphyrin complexes. The spectroscopic and redox properties of the resulting particle are consistent with the presence of 80 site-isolated bis(histidine)-bound heme centers, comprising a polyvalent b-type cytochrome mimic.
Prasuhn
Duane E
DE
Department of Chemistry, The Scripps Research Institute, La Jolla, CA 92037, USA.
Kuzelka
Jane
J
Strable
Erica
E
Udit
Andrew K
AK
Cho
So-Hye
SH
Lander
Gabriel C
GC
Quispe
Joel D
JD
Diers
James R
JR
Bocian
David F
DF
Potter
Clint
C
Carragher
Bridget
B
Finn
M G
MG
D001483:Base Sequence; D002213:Capsid / Q000737:chemistry / Q000378:metabolism*; D002850:Chromatography, Gel; D020285:Cryoelectron Microscopy; D017931:DNA Primers; D006418:Heme / Q000378:metabolism*; D006515:Hepatitis B virus / Q000378:metabolism*; D006639:Histidine / Q000737:chemistry / Q000378:metabolism*; D009842:Oligopeptides / Q000737:chemistry / Q000378:metabolism*; D013059:Spectrum Analysis, Raman
D017931:DNA Primers; C471213:His-His-His-His-His-His; D009842:Oligopeptides; D006418:Heme; D006639:Histidine