Literature DB >> 1856858

Crystallographic data for H-protein from the glycine decarboxylase complex.

L Sieker1, C Cohen-Addad, M Neuburger, R Douce.   

Abstract

The H-protein is the pivotal enzyme of the glycine decarboxylase complex responsible for the oxidation of glycine by mitochondria. It has been extracted and purified from pea leaf mitochondria (Pisum sativum). Its molecular weight, based on the amino acid sequence, is 13.3 kDa and it crystallizes in the space group P3(1)21 (or its enantiomorph P3(2)21) with a = b = 57.14 (3) A, c = 137.11 (11) A. The crystals diffract until at least 3.5 A resolution.

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Year:  1991        PMID： 1856858     DOI： 10.1016/0022-2836(91)90007-s

Source DB:  PubMed          Journal:  J Mol Biol        ISSN： 0022-2836            Impact factor:   5.469


  3 in total

1.  X-ray structure determination at 2.6-A resolution of a lipoate-containing protein: the H-protein of the glycine decarboxylase complex from pea leaves.

Authors:  S Pares; C Cohen-Addad; L Sieker; M Neuburger; R Douce
Journal:  Proc Natl Acad Sci U S A       Date:  1994-05-24       Impact factor: 11.205

Review 2.  Glycine decarboxylase: protein chemistry and molecular biology of the major protein in leaf mitochondria.

Authors:  D J Oliver; R Raman
Journal:  J Bioenerg Biomembr       Date:  1995-08       Impact factor: 2.945

3.  Prediction of the three-dimensional structures of the biotinylated domain from yeast pyruvate carboxylase and of the lipoylated H-protein from the pea leaf glycine cleavage system: a new automated method for the prediction of protein tertiary structure.

Authors:  S M Brocklehurst; R N Perham
Journal:  Protein Sci       Date:  1993-04       Impact factor: 6.725
  3 in total

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