NMR structure of the hypothetical protein AQ‐1857 encoded by the Y157 gene from <i>Aquifex aeolicus</i> reveals a novel protein fold

Xu, Duanxiang; Liu, Gaohua; Xiao, Rong; Acton, T.B.; Goldsmith-Fischman, Sharon; Montelione, Gaetano T.; Szyperski, Thomas

doi:10.1002/prot.10424

Cited by 7 publications

(8 citation statements)

References 16 publications

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“…42 The NESG Consortium has also previously reported the NMR structure of the related YgdK protein from E. coli (NESG target ER75, PDB id 1NI7), and an NMR structure of an IscA homolog from Aquifex aeolicus (NESG target QR6). 43 Taken in combination, these results demonstrate the complementary use of crystallography and NMR by a structural genomics consortium to characterize the structural and functional biology of proteins involved in the essential metabolic process of Fe-S cluster assembly. Figure 2 shows a gel-filtration chromatography analysis of the SufE crystallization stock monitored by static light-scattering and refractive index detectors.…”

Section: Introductionmentioning

confidence: 90%

The SufE Sulfur-acceptor Protein Contains a Conserved Core Structure that Mediates Interdomain Interactions in a Variety of Redox Protein Complexes

Goldsmith-Fischman

Kuzin

Edstrom

et al. 2004

Journal of Molecular Biology

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Section: Introductionmentioning

confidence: 90%

The SufE Sulfur-acceptor Protein Contains a Conserved Core Structure that Mediates Interdomain Interactions in a Variety of Redox Protein Complexes

Goldsmith-Fischman

Kuzin

Edstrom

et al. 2004

Journal of Molecular Biology

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“…From this point of view, it should be noted that two corresponding loops of apo form of A. aeolicus IscA seem to be flexibly disordered to some extent in the NMR solution structure. 24 Such conformational flexibilities of the two pseudo-symmetric loops, one of which contains one invariant Cys residue, might make the unique asymmetric arrangement of IscA dimer possible.…”

Section: Unique Asymmetric Arrangement Of Isca Dimermentioning

confidence: 99%

The Asymmetric IscA Homodimer with an Exposed [2Fe-2S] Cluster Suggests the Structural Basis of the Fe-S Cluster Biosynthetic Scaffold

Morimoto

Yamashita

Kondou

et al. 2006

Journal of Molecular Biology

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“…All three of the conserved cysteine residues are essential for function based on in vivo yeast mutagenesis studies (17;18). Crystal structures have been reported for the apo forms of Escherichia coli IscA (19;20) and SufA (21) and an NMR structure has been reported for Aquifex aeolicus IscA (22). The structures all show a novel protein fold, but were of limited utility for addressing the site for Fe or Fe-S cluster binding as the N-terminal C-G-C motif was generally not observed, presumably because of conformational flexibility.…”

Section: Introductionmentioning

confidence: 99%

Spectroscopic and Functional Characterization of Iron-Bound Forms of Azotobacter vinelandii^NifIscA

et al. 2012

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The ability of Azotobacter vinelandii NifIscA to bind Fe has been investigated to assess the role of Fe-bound forms in NIF-specific Fe-S cluster biogenesis. NifIscA is shown to bind one Fe(III) or one Fe(II) per homodimer and the spectroscopic and redox properties of both the Fe(III)- and Fe(II)-bound forms have been characterized using the UV-visible absorption, CD and VTMCD, EPR, Mössbauer and resonance Raman spectroscopies. The results reveal a rhombic intermediate-spin (S = 3/2) Fe(III) center (E/D = 0.33, D = 3.5 ± 1.5cm−1) that is most likely 5-coordinate with two or three cysteinate ligands and a rhombic high spin (S = 2) Fe(II) center (E/D = 0.28, D = 7.6 cm−1) with properties similar to reduced rubredoxins or rubredoxin variants with three cysteinate and one or two oxygenic ligands. Iron-bound NifIscA undergoes reversible redox cycling between the Fe(III)/Fe(II) forms with a midpoint potential of +36 ±15 mV at pH 7.8 (versus NHE). L-cysteine is effective in mediating release of free Fe(II) from both the Fe(II)- and Fe(III)-bound forms of NifIscA. Fe(III)-bound NifIscA was also shown to a competent iron source for in vitro NifS-mediated [2Fe-2S] cluster assembly on the N-terminal domain of NifU, but the reaction occurs via cysteine-mediated release of free Fe(II) rather than direct iron transfer. The proposed roles of A-type proteins in storing Fe under aerobic growth conditions and serving as iron donors for cluster assembly on U-type scaffold proteins or maturation of biological [4Fe-4S] centers are discussed in light of these results.

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NMR structure of the hypothetical protein AQ‐1857 encoded by the Y157 gene from Aquifex aeolicus reveals a novel protein fold

Cited by 7 publications

References 16 publications

The SufE Sulfur-acceptor Protein Contains a Conserved Core Structure that Mediates Interdomain Interactions in a Variety of Redox Protein Complexes

The SufE Sulfur-acceptor Protein Contains a Conserved Core Structure that Mediates Interdomain Interactions in a Variety of Redox Protein Complexes

The Asymmetric IscA Homodimer with an Exposed [2Fe-2S] Cluster Suggests the Structural Basis of the Fe-S Cluster Biosynthetic Scaffold

Spectroscopic and Functional Characterization of Iron-Bound Forms of Azotobacter vinelandii^NifIscA

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NMR structure of the hypothetical protein AQ‐1857 encoded by the Y157 gene from Aquifex aeolicus reveals a novel protein fold

Cited by 7 publications

References 16 publications

The SufE Sulfur-acceptor Protein Contains a Conserved Core Structure that Mediates Interdomain Interactions in a Variety of Redox Protein Complexes

The SufE Sulfur-acceptor Protein Contains a Conserved Core Structure that Mediates Interdomain Interactions in a Variety of Redox Protein Complexes

The Asymmetric IscA Homodimer with an Exposed [2Fe-2S] Cluster Suggests the Structural Basis of the Fe-S Cluster Biosynthetic Scaffold

Spectroscopic and Functional Characterization of Iron-Bound Forms of Azotobacter vinelandiiNifIscA

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Spectroscopic and Functional Characterization of Iron-Bound Forms of Azotobacter vinelandii^NifIscA