Crystallization and crystallographic analysis of the apo form of the orange protein (ORP) from<i>Desulfovibrio gigas</i>

Najmudin, Shabir; Bonifacio, C.; Duarte, Américo G.; Pualeta, Sofia R.; Moura, Isabel; Moura, José J. G.; Romão, Maria João

doi:10.1107/s1744309109023392

Cited by 10 publications

(26 citation statements)

References 15 publications

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“…To the best of our knowledge, this is the first report of 3‐NT formation by a Ni II ‐ATCUN in the presence of the NO 2 − /SO 3 2− /O 2 system. For this experiment, we used fusion orange protein (ATCUN‐ORP) as an in vitro model complex containing ATCUN tag at the N‐terminus (ASH) and native Tyr 75 located in cluster binding region of ATCUN‐ORP (Figure ) . Recently, we have reported that cluster formation in ORP occur by protein–protein interaction in head‐to‐tail fashion, in which the N‐terminus metal‐binding ATCUN motif comes to the cluster‐binding region, in which Tyr residues are affected through pseudocontact .…”

Section: Figurementioning

confidence: 99%

“…Structures of apo‐ATCUN‐ORP ( D. gigas ) are deduced from PDB file 2wfb, see Ref. . Ni‐ATCUN catalyzed Tyr to 3‐NO 2 ‐Tyr in the presence of Na 2 NO 2 /Na 2 SO 3 /O 2 .…”

Section: Figurementioning

confidence: 99%

“…For this experiment,w eu sed fusion orange protein (ATCUN-ORP) as an in vitro model complex containing ATCUN tag at the N-terminus (ASH) and native Tyr 75 located in cluster binding region of ATCUN-ORP ( Figure 1). [20,21] Recently,w eh ave reported that cluster formation in ORP occur by protein-protein interaction in head-to-tail fashion, in which the N-terminus metal-binding ATCUN motif comes to the cluster-binding region, in whichT yr residues are affected through pseudocontact. [20] Therefore, taking advantage of this model system, Ni II -ATCUN-ORP was synthesized in the presence of NiCl 2 and apo-ATCUN-ORP at 1:1r atio and characterized by UV/Vis absorption and 1 HNMR spectroscopic studies.…”

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confidence: 99%

“…Crystal structureo fa po-ATCUN-ORPshowing only His 3 (ATCUN tag = ASH 3 -) and nativeT yr 75/42 residues. Highlighted metal-binding region (reddish-orange) containingc onserved residues D 21 PRFGRA 27 ,H 53 GAGIN 58 , and L 72 TGYVGPKAF 81 .S tructures of apo-ATCUN-ORP (D. gigas)are deduced from PDB file 2wfb,s ee Ref [21]…”

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confidence: 99%

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Ni^II‐ATCUN‐Catalyzed Tyrosine Nitration in the Presence of Nitrite and Sulfite

Maiti

Maia

Moura

et al. 2019

Chemistry A European J

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The nitration of tyrosine residues in proteins represents a specific footprint of the formation of reactive nitrogen species (RNS) in vivo. Here, the fusion product of orange protein (ATCUN‐ORP) was used as an in vitro model system containing an amino terminal Cu(II)‐ and Ni(II)‐binding motif (ATCUN) tag at the N‐terminus and a native tyrosine residue in the metal‐cofactor‐binding region for the formation of 3‐NO2‐Tyr (3‐NT). It is shown that NiII‐ATCUN unusually performs nitration of tyrosine at physiological pH in the presence of the NO2−/SO32−/O2 system, which is revealed by a characteristic absorbance band at 430 nm in basic medium and 350 nm in acidic medium (fingerprint of 3‐NT). Kinetics studies showed that the formation of 3‐NT depends on sulfite concentration over nitrite concentration suggesting key intermediate products, identified as oxysulfur radicals, which are detected by spin‐trap EPR study by using 5,5‐dimethyl‐1‐pyrroline‐N‐oxide (DMPO). This study describes a new route in the formation of 3‐NT, which is proposed to be linked with the sulfur metabolism pathway associated with the progression of disease occurrence in vivo.

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Section: Figurementioning

confidence: 99%

“…Structures of apo‐ATCUN‐ORP ( D. gigas ) are deduced from PDB file 2wfb, see Ref. . Ni‐ATCUN catalyzed Tyr to 3‐NO 2 ‐Tyr in the presence of Na 2 NO 2 /Na 2 SO 3 /O 2 .…”

Section: Figurementioning

confidence: 99%

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confidence: 99%

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confidence: 99%

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Ni^II‐ATCUN‐Catalyzed Tyrosine Nitration in the Presence of Nitrite and Sulfite

Maiti

Maia

Moura

et al. 2019

Chemistry A European J

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“…In the article by Najmudin et al (2009) the name of one of the authors was given incorrectly: the name Pualeta should be spelt Pauleta. The correct list of authors is S. Najmudin, C. Bonifá cio, A. G. Duarte, S. R. Pauleta, I. Moura, J. J. G. Moura and M. J. Romã o.…”

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Crystallization and crystallographic analysis of the apo form of the orange protein (ORP) fromDesulfovibrio gigas. Corrigendum

Moura

Pauleta

et al. 2009

Acta Cryst Sect F

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Orange protein from Desulfovibrio alaskensis G20: insights into the Mo–Cu cluster protein-assisted synthesis

et al. 2016

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A novel metalloprotein containing a unique [S2MoS2CuS2MoS2](3-) cluster, designated as Orange Protein (ORP), was isolated for the first time from Desulfovibrio gigas, a sulphate reducer. The orp operon is conserved in almost all sequenced Desulfovibrio genomes and in other anaerobic bacteria, however, so far D. gigas ORP had been the only ORP characterized in the literature. In this work, the purification of another ORP isolated form Desulfovibrio alaskensis G20 is reported. The native protein is monomeric (12443.8 ± 0.1 Da by ESI-MS) and contains also a MoCu cluster with characteristic absorption bands at 337 and 480 nm, assigned to S-Mo charge transfer bands. Desulfovibrio alaskensis G20 recombinant protein was obtained in the apo-form from E. coli. Cluster reconstitution studies and UV-visible titrations with tetrathiomolybdate of the apo-ORP incubated with Cu ions indicate that the cluster is incorporated in a protein metal-assisted synthetic mode and the protein favors the 2Mo:1Cu stoichiometry. In Desulfovibrio alaskensis G20, the orp genes are encoded by a polycistronic unit composed of six genes whereas in Desulfovibrio vulgaris Hildenborough the same genes are organized into two divergent operons, although the composition in genes is similar. The gene expression of ORP (Dde_3198) increased 6.6 ± 0.5 times when molybdate was added to the growth medium but was not affected by Cu(II) addition, suggesting an involvement in molybdenum metabolism directly or indirectly in these anaerobic bacteria.

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Crystallization and crystallographic analysis of the apo form of the orange protein (ORP) fromDesulfovibrio gigas

Cited by 10 publications

References 15 publications

Ni^II‐ATCUN‐Catalyzed Tyrosine Nitration in the Presence of Nitrite and Sulfite

Ni^II‐ATCUN‐Catalyzed Tyrosine Nitration in the Presence of Nitrite and Sulfite

Crystallization and crystallographic analysis of the apo form of the orange protein (ORP) fromDesulfovibrio gigas. Corrigendum

Orange protein from Desulfovibrio alaskensis G20: insights into the Mo–Cu cluster protein-assisted synthesis

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Crystallization and crystallographic analysis of the apo form of the orange protein (ORP) fromDesulfovibrio gigas

Cited by 10 publications

References 15 publications

NiII‐ATCUN‐Catalyzed Tyrosine Nitration in the Presence of Nitrite and Sulfite

NiII‐ATCUN‐Catalyzed Tyrosine Nitration in the Presence of Nitrite and Sulfite

Crystallization and crystallographic analysis of the apo form of the orange protein (ORP) fromDesulfovibrio gigas. Corrigendum

Orange protein from Desulfovibrio alaskensis G20: insights into the Mo–Cu cluster protein-assisted synthesis

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Ni^II‐ATCUN‐Catalyzed Tyrosine Nitration in the Presence of Nitrite and Sulfite

Ni^II‐ATCUN‐Catalyzed Tyrosine Nitration in the Presence of Nitrite and Sulfite