Note_DisulfideBonds – DisulfideBonds

Name
WID Note_DisulfideBonds
Name DisulfideBonds
 
Comments
Comments Disulfide bonds reconstructed by a combination 1) primary literature, 2) homology to observed disulfide bonds [PUB_0096], and 3) computational prediction for all proteins using DiANNA v1.1 software [PUB_0299]. Cytoplasm is a reducing environment, thus few disulfide bonds form there [PUB_0300]. Periplasm and extracellular space are not reducing environments, and disulfide bonds are more commonly found there [PUB_0300]. In eukaryotes disulfide bonds are introduced by the chaperone protein disulfide isomerase (PDI) in the endoplasmic reticulum [PUB_0300]. Spontaneous disulfide bond formation is slow and error-prone [PUB_0300]. E. coli has a periplasmic enzyme (dsbA, b1185) with similar properties to PDI [PUB_0300]. M. genitalium has no dsbA ortholog. dsbA is not an essential gene [PUB_0300]. Disulfide bonds have been observed in M. fermentans P29 adhesin [PUB_0301] and M. pneumoniae OsmC [PUB_0302]. Thioredoxin plays a role in reducing disulfide bonds [PUB_0304]. TrxB mutants display additional cytoplasmic disulfide bonds [PUB_0145]. Formation of disulfide bonds in exported proteins occurs only during or after their export from the cytoplasm [PUB_0145]. Oxidized thioredoxin is not believed to contribute to disulfide bond formation [PUB_0145].
References
  1. Ben-Menachem G, Himmelreich R, Herrmann R, Aharonowitz Y, Rottem S. The thioredoxin reductase system of mycoplasmas. Microbiology 143 ( Pt 6), 1933-40 (1997). WholeCell: PUB_0304, PubMed: 9202470

  2. Choi IG, Shin DH, Brandsen J, Jancarik J, Busso D, Yokota H, Kim R, Kim SH. Crystal structure of a stress inducible protein from Mycoplasma pneumoniae at 2.85 A resolution. J Struct Funct Genomics 4, 31-4 (2003). WholeCell: PUB_0302, PubMed: 12943365

  3. Ferrè F, Clote P. DiANNA 1.1: an extension of the DiANNA web server for ternary cysteine classification. Nucleic Acids Res 34, W182-5 (2006). WholeCell: PUB_0299, PubMed: 16844987

  4. Leigh SA, Wise KS. Identification and functional mapping of the Mycoplasma fermentans P29 adhesin. Infect Immun 70, 4925-35 (2002). WholeCell: PUB_0301, PubMed: 12183538

  5. Lesniak J, Barton WA, Nikolov DB. Structural and functional features of the Escherichia coli hydroperoxide resistance protein OsmC. Protein Sci 12, 2838-43 (2003). WholeCell: PUB_0145, PubMed: 14627744

  6. ... 2 more

  7. Pugsley AP. The complete general secretory pathway in gram-negative bacteria. Microbiol Rev 57, 50-108 (1993). WholeCell: PUB_0300, PubMed: 8096622

  8. UniProt Consortium. The Universal Protein Resource (UniProt) 2009. Nucleic Acids Res 37, D169-74 (2009). WholeCell: PUB_0096, PubMed: 18836194, URL: http://www.uniprot.org/uniprot/

 
Metadata
Created 2012-10-01 15:07:34
Last updated 2012-10-01 15:13:57