Literature DB >> 6267021

On the evolutionary relationship of the 4-alpha-helical heme proteins. The comparison of cytochrome b562 and cytochrome c'.

P C Weber, F R Salemme, F S Mathews, P H Bethge.   

Abstract

The atomic models of the cytochrome b562 and cytochrome c' monomers have been compared. When the respective heme groups are superimposed, the four alpha-helices of each nearly coincide. Four aromatic side chains, including the heme ligands, and a methionine occur in spatially equivalent positions in contact with the heme groups. This structural evidence suggests that the two cytochrome families may have diverged from a common molecular ancestor.

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Year:  1981        PMID: 6267021

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  2 in total

1.  Sequence-structure matching in globular proteins: application to supersecondary and tertiary structure determination.

Authors:  A Godzik; J Skolnick
Journal:  Proc Natl Acad Sci U S A       Date:  1992-12-15       Impact factor: 11.205

2.  Refolding of cytochrome b562 and its structural stabilization by introducing a disulfide bond.

Authors:  Y Kobayashi; H Sasabe; N Saitô
Journal:  J Protein Chem       Date:  1993-04
  2 in total

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