Crystal Structure of the 16 Heme Cytochrome from Desulfovibrio gigas: A Glycosylated Protein in a Sulphate-reducing Bacterium

Santos‐Silva, Teresa; Dias, João M.; Dolla, Alain; Durand, Marie-Claire; Gonçalves, Leônor; Lampreia, Jorge; Moura, Isabel; Romão, Maria João

doi:10.1016/j.jmb.2007.04.055

Cited by 23 publications

(21 citation statements)

References 62 publications

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“…The amino acid sequence of hHyal-1 contains three predicted N-glycosylation sites at Asn-99, Asn-216, and Asn-350; thus the estimated average N-glycan mass is 1,169 Da per site, in agreement with previously reported biantennary carbohydrates linked to proteins expressed in Drosophila cells (Chao, Muthukumar, & Herzberg, 2007). The difference between the calculated (66,553 Da) and measured mass (67,166 Da) for the 16 heme cytochrome from Desulfovibrio gigas measured by Santos-Silva et al (2007) allowed the authors to conclude that the protein probably contained three GlcNAc residues. Miller et al (2008) have measured the mass of a flagellin mutant as 40,197 (AE10) Da, which would correspond to the mass of flagellin with two deoxyhexose substituents each with a mass of 146 Da.…”

Section: Analysis Of Carbohydrates and Glycoconjugatessupporting

confidence: 87%

Analysis of carbohydrates and glycoconjugates by matrix‐assisted laser desorption/ionization mass spectrometry: An update for 2007–2008

Harvey

2011

Mass Spectrometry Reviews

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This review is the fifth update of the original review, published in 1999, on the application of MALDI mass spectrometry to the analysis of carbohydrates and glycoconjugates and brings coverage of the literature to the end of 2008. The first section of the review covers fundamental studies, fragmentation of carbohydrate ions, use of derivatives and new software developments for analysis of carbohydrate spectra. Among newer areas of method development are glycan arrays, MALDI imaging and the use of ion mobility spectrometry. The second section of the review discusses applications of MALDI MS to the analysis of different types of carbohydrate. Specific compound classes that are covered include carbohydrate polymers from plants, N- and O-linked glycans from glycoproteins, biopharmaceuticals, glycated proteins, glycolipids, glycosides and various other natural products. There is a short section on the use of MALDI mass spectrometry for the study of enzymes involved in glycan processing and a section on the use of MALDI MS to monitor products of the chemical synthesis of carbohydrates with emphasis on carbohydrate-protein complexes and glycodendrimers. Corresponding analyses by electrospray ionization now appear to outnumber those performed by MALDI and the amount of literature makes a comprehensive review on this technique impractical. However, most of the work relating to sample preparation and glycan synthesis is equally relevant to electrospray and, consequently, those proposing analyses by electrospray should also find material in this review of interest.

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Section: Analysis Of Carbohydrates and Glycoconjugatessupporting

confidence: 87%

Analysis of carbohydrates and glycoconjugates by matrix‐assisted laser desorption/ionization mass spectrometry: An update for 2007–2008

Harvey

2011

Mass Spectrometry Reviews

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“…In bacteria and archaea, dedicated multicomponent pathways known as Systems I (CCM) and/or II (CcsBA) traffic and attach the heme (9 -16). In prokaryotes, many c-type cytochromes exist in addition to monoheme proteins (17)(18)(19)(20). These are all matured by Systems I and II, consistent with the proposal that only the CXXCH motif is recognized (21)(22)(23)(24).…”

supporting

confidence: 81%

“…2, A-C). Ser 16 and Gln 17 were substituted with alanine residues (S16A/Q17A) because the equivalent positions in bacterial cytochromes are variable. These substitutions resulted in near-wild-type (WT) levels of cyt c (Fig.…”

Section: Resultsmentioning

confidence: 99%

Molecular Basis Behind Inability of Mitochondrial Holocytochrome c Synthase to Mature Bacterial Cytochromes

Babbitt

Hsu

Kranz

2016

Journal of Biological Chemistry

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Mitochondrial holocytochrome c synthase (HCCS) is required for cytochrome c (cyt c) maturation and therefore respiration. HCCS efficiently attaches heme via two thioethers to CXXCH of mitochondrial but not bacterial cyt c even though they are functionally conserved. This inability is due to residues in the bacterial cyt c N terminus, but the molecular basis is unknown. Human cyts c with deletions of single residues in ␣ helix-1, which mimic bacterial cyt c, are poorly matured by human HCCS. Focusing on ⌬M13 cyt c, we co-purified this variant with HCCS, demonstrating that HCCS recognizes the bacterial-like cytochrome. Although an HCCS-WT cyt c complex contains two covalent links, HCCS-⌬M13 cyt c contains only one thioether attachment. Using multiple approaches, we show that the single attachment is to the second thiol of C 15 SQC 18 H, indicating that ␣ helix-1 is required for positioning the first cysteine for covalent attachment, whereas the histidine of CXXCH positions the second cysteine. Modeling of the N-terminal structure suggested that the serine residue (of CSQCH) would be anchored where the first cysteine should be in ⌬M13 cyt c. An engineered cyt c with a CQCH motif in the ⌬M13 background is matured at higher levels (2-3-fold), providing further evidence for ␣ helix-1 positioning the first cysteine. Bacterial cyt c biogenesis pathways (Systems I and II) appear to recognize simply the CXXCH motif, not requiring ␣ helix-1. Results here explain mechanistically how HCCS (System III) requires an extended region adjacent to CXXCH for maturation.

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“…Desulfovibrio species were excluded from these analyses because they do not possess obvious PglFED orthologs. This is supported by x-ray crystallography data demonstrating that the reducing end sugar of Desulfovibrio gigas is GlcNAc (29).…”

Section: Evolutionary Perspectivementioning

confidence: 68%

“…6). In addition, a subset of Deltaproteobacteria, including Desulfovibrio species, also possess the N-glycan pathway (28,29).…”

Section: Bacterial N-linked Protein Glycosylation: An Updatementioning

confidence: 99%

Bacterial Protein N-Glycosylation: New Perspectives and Applications

Nothaft

Szymanski

2013

Journal of Biological Chemistry

144

123

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Protein glycosylation is widespread throughout all three domains of life. Bacterial protein N-glycosylation and its application to engineering recombinant glycoproteins continue to be actively studied. Here, we focus on advances made in the last 2 years, including the characterization of novel bacterial N-glycosylation pathways, examination of pathway enzymes and evolution, biological roles of protein modification in the native host, and exploitation of the N-glycosylation pathways to create novel vaccines and diagnostics.

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Crystal Structure of the 16 Heme Cytochrome from Desulfovibrio gigas: A Glycosylated Protein in a Sulphate-reducing Bacterium

Cited by 23 publications

References 62 publications

Analysis of carbohydrates and glycoconjugates by matrix‐assisted laser desorption/ionization mass spectrometry: An update for 2007–2008

Analysis of carbohydrates and glycoconjugates by matrix‐assisted laser desorption/ionization mass spectrometry: An update for 2007–2008

Molecular Basis Behind Inability of Mitochondrial Holocytochrome c Synthase to Mature Bacterial Cytochromes

Bacterial Protein N-Glycosylation: New Perspectives and Applications

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