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

作者信息

Sieker L, Cohen-Addad C, Neuburger M, Douce R

机构信息

CNRS, URA 1333, Centre d'Etudes Nucléaires, Grenoble, France.

出版信息

J Mol Biol. 1991 Jul 20;220(2):223-4. doi: 10.1016/0022-2836(91)90007-s.

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

摘要

相似文献

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Crystallographic data for H-protein from the glycine decarboxylase complex.
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2
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引用本文的文献

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2
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.酵母丙酮酸羧化酶生物素化结构域及豌豆叶甘氨酸裂解系统脂酰化H蛋白三维结构的预测：一种预测蛋白质三级结构的新自动化方法
Protein Sci. 1993 Apr;2(4):626-39. doi: 10.1002/pro.5560020413.
3
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.
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