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Bacterioferritin from Mycobacterium smegmatis contains zinc in its di‐nuclear site
Author(s) -
Janowski Robert,
AuerbachNevo Tamar,
Weiss Manfred S.
Publication year - 2008
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.034819.108
Subject(s) - mycobacterium smegmatis , zinc , chemistry , crystallography , mycobacterium tuberculosis , medicine , tuberculosis , organic chemistry , pathology
Bacterioferritins, also known as cytochrome b 1 , are oligomeric iron‐storage proteins consisting of 24 identical amino acid chains, which form spherical particles consisting of 24 subunits and exhibiting 432 point‐group symmetry. They contain one haem b molecule at the interface between two subunits and a di‐nuclear metal binding center. The X‐ray structure of bacterioferritin from Mycobacterium smegmatis ( Ms ‐Bfr) was determined to a resolution of 2.7 Å in the monoclinic space group C 2. The asymmetric unit of the crystals contains 12 protein molecules: five dimers and two half‐dimers located along the crystallographic twofold axis. Unexpectedly, the di‐nuclear metal binding center contains zinc ions instead of the typically observed iron ions in other bacterioferritins.