NMR structure of the hypothetical protein NMA1147 from <i>Neisseria meningitidis</i> Reveals a distinct 5‐helix bundle

Liu, Gaohua; Sukumaran, Dinesh K.; Xu, Duanxiang; Chiang, Yiwen; Acton, Thomas; Goldsmith-Fischman, Sharon; Montelione, Gaetano T.; Szyperski, Thomas

doi:10.1002/prot.20009

Cited by 7 publications

(11 citation statements)

References 15 publications

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“…The remaining DALI hits were of low significance (Z-scores < 4.2), a finding which confirms the original assessment 14 that the five-helix bundle first described for NMA1147 14 is of ‘distinct’ nature.…”

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confidence: 73%

Solution NMR Structure of Yeast Succinate Dehydrogenase Flavinylation Factor Sdh5 Reveals a Putative Sdh1 Binding Site

et al. 2012

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The yeast mitochondrial protein Sdh5 is required for the covalent attachment of flavin adenine dinucleotide (FAD) to protein Sdh1, a subunit of the hetero-tetrameric enzyme succinate dehydrogenase (SDH). The NMR structure of Sdh5 represents the first eukaryotic structure of the Pfam family PF03937 and reveals a conserved surface region, which likely represents a putative Sdh1-Sdh5 interaction interface. Point mutations in this region result in the loss of covalent flavinylation of Sdh1. Moreover, backbone chemical shift perturbation measurements showed that Sdh5 does not bind FAD in vitro, indicating that it does not function as simple cofactor transporter in vivo.

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confidence: 73%

Solution NMR Structure of Yeast Succinate Dehydrogenase Flavinylation Factor Sdh5 Reveals a Putative Sdh1 Binding Site

et al. 2012

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“…Based on sequence homology, Sdh5 belongs to a large protein superfamily now classified as “flavinylation factors of SDH” or “Sdh5 superfamily.” The structures of three other proteins belonging to this family are also available as a result of structural genomics initiatives: YgfY from E. coli [57] along with two other proteins that are currently unnamed, NMA1147 from N. meningitides [58], and VC2471 from Vibrio cholerae . Compared to its bacterial counterparts, the eukaryotic Sdh5 has an extra stretch of residues comprised essentially of a strand at its amino terminus (after cleavage of the predicted mitochondrial targeting peptide [59]).…”

Section: 0 In Vivo Flavinylation Of Sdh1 Requires Other Factorsmentioning

confidence: 99%

Emerging concepts in the flavinylation of succinate dehydrogenase

Kim

Winge

2013

Biochimica et Biophysica Acta (BBA) - Bioenergetics

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The Succinate Dehydrogenase (SDH) heterotetrameric complex catalyzes the oxidation of succinate to fumarate in the tricarboxylic acid (TCA) cycle and in the aerobic respiratory chains of eukaryotes and bacteria. Essential in this catalysis, is the covalently-linked cofactor flavin adenine dinucleotide (FAD) in subunit1 (Sdh1) of the SDH enzyme complex. The mechanism of FAD insertion and covalent attachment to Sdh1 is unknown. Our working concept of this flavinylation process has relied mostly on foundational works from the 1990s ago and by applying the principles learned from other enzymes containing a similarly linked FAD. The discovery of the flavinylation factor Sdh5, however, has provided new insight into the possible mechanism associated with Sdh1 flavinylation, bringing into question the autocatalytic mechanism associated with other flavoenzymes. This review focuses on encapsulating prior and recent advances towards understanding the mechanism associated with flavinylation of Sdh1 and how this flavinylation process affects the overall assembly of SDH.

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“…The crystal structure of YgfY was determined at 1.2 Å resolution as a part of our structural genomics project (http://s2f.umbi.umd.edu), revealing a five‐helix fold similar to that of the homologous protein NMA1147 from Neisseria meningitidis (30% identity) determined recently by NMR methods 4. Yet, there are inconsistencies in the details of these two structures that reflect the different levels of accuracy of the two methods of structure determination.…”

Section: Introductionmentioning

confidence: 99%

Crystal structure of the YgfY from Escherichia coli, a protein that may be involved in transcriptional regulation

et al. 2004

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NMR structure of the hypothetical protein NMA1147 from Neisseria meningitidis Reveals a distinct 5‐helix bundle

Cited by 7 publications

References 15 publications

Solution NMR Structure of Yeast Succinate Dehydrogenase Flavinylation Factor Sdh5 Reveals a Putative Sdh1 Binding Site

Solution NMR Structure of Yeast Succinate Dehydrogenase Flavinylation Factor Sdh5 Reveals a Putative Sdh1 Binding Site

Emerging concepts in the flavinylation of succinate dehydrogenase

Crystal structure of the YgfY from Escherichia coli, a protein that may be involved in transcriptional regulation

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