2008
DOI: 10.1016/j.jmb.2007.10.023
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Structural Studies on the Second Mycobacterium smegmatis Dps: Invariant and Variable Features of Structure, Assembly and Function

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Cited by 61 publications
(82 citation statements)
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“…4,5 The structures of the enzyme in the CoA complex and in the complexes involving AMPPNP and ADP also show significant differences. 4,5 We have been exploring the structures and interactions of PanK from Mycobacterium tuberculosis (MtPanK) as part of a program in this laboratory [6][7][8][9][10][11][12] and an international effort involving structural studies on mycobacterial proteins. [13][14][15][16][17] The CoA complex of MtPanK has a structure very similar to that of the corresponding EcPanK complex.…”
Section: Introductionmentioning
confidence: 99%
“…4,5 The structures of the enzyme in the CoA complex and in the complexes involving AMPPNP and ADP also show significant differences. 4,5 We have been exploring the structures and interactions of PanK from Mycobacterium tuberculosis (MtPanK) as part of a program in this laboratory [6][7][8][9][10][11][12] and an international effort involving structural studies on mycobacterial proteins. [13][14][15][16][17] The CoA complex of MtPanK has a structure very similar to that of the corresponding EcPanK complex.…”
Section: Introductionmentioning
confidence: 99%
“…Since this pioneer study, many different Dps proteins have been characterized. These proteins are structurally conserved and widely distributed in prokaryotes (8,9). Unlike typical ferritins that have 24 subunits and 432 symmetry, Dps proteins assemble in a quasispherical dodecamer with 23 symmetry and can store ϳ500 iron atoms (4,10).…”
mentioning
confidence: 99%
“…MsDps1 is the only Dps that has been shown to exist as a trimer and a dodecamer in solution (55). MsDps2 on the other hand exhibits a stable dodecameric form in vitro (23). In this study, we have used as our model MsDps2 to study the mechanism of iron uptake and release in mycobacterial Dps molecules.…”
Section: Discussionmentioning
confidence: 99%
“…A search of TIGR database with the MsDps1 sequence led to the identification of the second Dps namely MsDps2 (23). MsDps1 has a long C-terminal tail rich in positively charged residues for DNA binding unlike MsDps2, which lacks any N-or C-terminal extensions, despite which it can still bind to DNA.…”
mentioning
confidence: 99%
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