Crystallographic analysis of the intact metal centres [3Fe-4S]1+/0 and [4Fe-4S]2+/1+ in a Zn2+-containing ferredoxin

Carlos Frazão; David Aragão; Ricardo Coelho; Sónia S. Leal; Cláudio M. Gomes; Miguel Teixeira; Maria Arménia Carrondo

doi:10.1016/j.febslet.2008.01.041

Crystallographic analysis of the intact metal centres [3Fe-4S]^1+/0 and [4Fe-4S]^2+/1+ in a Zn²⁺-containing ferredoxin

Carlos Frazão, David Aragão, Ricardo Coelho, Sónia S. Leal, Cláudio M. Gomes, Miguel Teixeira, Maria Arménia Carrondo

Instituto de Tecnologia Química e Biológica António Xavier (ITQB)

Research output: Contribution to journal › Article › peer-review

10 Citations (Scopus)

Abstract

Detailed structural models of di-cluster seven-iron ferredoxins constitute a valuable resource for folding and stability studies relating the metal cofactors' role in protein stability. The here reported, hemihedric twinned crystal structure at 2.0 Å resolution from Acidianus ambivalens ferredoxin, shows an integral 103 residues, physiologically relevant native form composed by a N-terminal extension comprising a His/Asp Zn²⁺ site and the ferredoxin (βαβ)₂ core, which harbours intact clusters I and II, a [3Fe-4S]^1+/0 and a [4Fe-4S]^2+/1+ centres. This is in contrast with the previously available ferredoxin structure from Sulfolofus tokodai, which was obtained from an artificial oxidative conversion with two [3Fe-4S]^1+/0 centres and poor definition around cluster II.

Original language	English
Pages (from-to)	763-767
Number of pages	5
Journal	FEBS Letters
Volume	582
Issue number	5
DOIs	https://doi.org/10.1016/j.febslet.2008.01.041
Publication status	Published - 5 Mar 2008

Keywords

Crystal twinning
Iron-sulfur proteins
Protein folding
Protein stability
Thermophiles
Zinc centres

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title = "Crystallographic analysis of the intact metal centres [3Fe-4S]1+/0 and [4Fe-4S]2+/1+ in a Zn2+-containing ferredoxin",

abstract = "Detailed structural models of di-cluster seven-iron ferredoxins constitute a valuable resource for folding and stability studies relating the metal cofactors' role in protein stability. The here reported, hemihedric twinned crystal structure at 2.0 {\AA} resolution from Acidianus ambivalens ferredoxin, shows an integral 103 residues, physiologically relevant native form composed by a N-terminal extension comprising a His/Asp Zn2+ site and the ferredoxin (βαβ)2 core, which harbours intact clusters I and II, a [3Fe-4S]1+/0 and a [4Fe-4S]2+/1+ centres. This is in contrast with the previously available ferredoxin structure from Sulfolofus tokodai, which was obtained from an artificial oxidative conversion with two [3Fe-4S]1+/0 centres and poor definition around cluster II.",

keywords = "Crystal twinning, Iron-sulfur proteins, Protein folding, Protein stability, Thermophiles, Zinc centres",

author = "Carlos Fraz{\~a}o and David Arag{\~a}o and Ricardo Coelho and Leal, {S{\'o}nia S.} and Gomes, {Cl{\'a}udio M.} and Miguel Teixeira and Carrondo, {Maria Arm{\'e}nia}",

year = "2008",

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AU - Frazão, Carlos

AU - Aragão, David

AU - Coelho, Ricardo

AU - Leal, Sónia S.

AU - Gomes, Cláudio M.

AU - Teixeira, Miguel

AU - Carrondo, Maria Arménia

PY - 2008/3/5

Y1 - 2008/3/5

N2 - Detailed structural models of di-cluster seven-iron ferredoxins constitute a valuable resource for folding and stability studies relating the metal cofactors' role in protein stability. The here reported, hemihedric twinned crystal structure at 2.0 Å resolution from Acidianus ambivalens ferredoxin, shows an integral 103 residues, physiologically relevant native form composed by a N-terminal extension comprising a His/Asp Zn2+ site and the ferredoxin (βαβ)2 core, which harbours intact clusters I and II, a [3Fe-4S]1+/0 and a [4Fe-4S]2+/1+ centres. This is in contrast with the previously available ferredoxin structure from Sulfolofus tokodai, which was obtained from an artificial oxidative conversion with two [3Fe-4S]1+/0 centres and poor definition around cluster II.

AB - Detailed structural models of di-cluster seven-iron ferredoxins constitute a valuable resource for folding and stability studies relating the metal cofactors' role in protein stability. The here reported, hemihedric twinned crystal structure at 2.0 Å resolution from Acidianus ambivalens ferredoxin, shows an integral 103 residues, physiologically relevant native form composed by a N-terminal extension comprising a His/Asp Zn2+ site and the ferredoxin (βαβ)2 core, which harbours intact clusters I and II, a [3Fe-4S]1+/0 and a [4Fe-4S]2+/1+ centres. This is in contrast with the previously available ferredoxin structure from Sulfolofus tokodai, which was obtained from an artificial oxidative conversion with two [3Fe-4S]1+/0 centres and poor definition around cluster II.

KW - Crystal twinning

KW - Iron-sulfur proteins

KW - Protein folding

KW - Protein stability

KW - Thermophiles

KW - Zinc centres

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DO - 10.1016/j.febslet.2008.01.041

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SN - 0014-5793

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JF - FEBS Letters

IS - 5

ER -

Crystallographic analysis of the intact metal centres [3Fe-4S]^1+/0 and [4Fe-4S]^2+/1+ in a Zn²⁺-containing ferredoxin

Abstract

Keywords

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