2008
DOI: 10.1110/ps.034819.108
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Bacterioferritin from Mycobacterium smegmatis contains zinc in its di‐nuclear site

Abstract: 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 C2. The asymmetric unit of… Show more

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Cited by 26 publications
(35 citation statements)
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“…In the structures of Av Bfr reported by Swartz et al, 61 a Mg 2+ ion, coordinated by water molecules, was found within the B pores. In difference electron density maps of the Ms Bfr structure, 62 peaks too strong to be water molecules were found in all the B pores. Anomalous difference Fourier maps did not show peaks at the B sites, ruling out the presence of Zn or Fe ions.…”
Section: B Poresmentioning
confidence: 97%
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“…In the structures of Av Bfr reported by Swartz et al, 61 a Mg 2+ ion, coordinated by water molecules, was found within the B pores. In difference electron density maps of the Ms Bfr structure, 62 peaks too strong to be water molecules were found in all the B pores. Anomalous difference Fourier maps did not show peaks at the B sites, ruling out the presence of Zn or Fe ions.…”
Section: B Poresmentioning
confidence: 97%
“…67 The presence of a positive charge in the central and narrowest section of threefold pores in bacterial Ftn strongly suggests that, in contrast to their function in eukaryotic Ftn, threefold channels in bacterial and Bfrs do not function to enable the traffic of Fe(II). 62,64 In this regard, it is noteworthy that phosphate is an integral component of the core mineral in bacterial Ftn, where it is present in nearly a 1:1 ratio with iron. [124][125][126] Hence, it has been pointed out that the phosphate needed to support the growth of core mineral in Bfrs and bacterial Ftns may traffic across the protein shell via threefold pores.…”
Section: A Threefold Poresmentioning
confidence: 99%
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“…In contrast, the present study includes structural characterization of Mtb-BfrA that is bound to fully intact heme with bis-methionyl coordination. Although structural models of heme bound bacterioferritin have been previously reported [1,[17][18][19][20][21][22], this is the first systematic study whereby the H-bonding network is documented with varying degrees of heme incorporation. Furthermore, we demonstrate that the presence of heme does not significantly alter Mtb-BfrA ferroxidase activity.…”
Section: Introductionmentioning
confidence: 94%