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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
11
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pubmed:dateCreated |
1994-6-27
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pubmed:abstractText |
H-protein, a lipoic acid-containing protein of the glycine decarboxylase (EC 1.4.4.2) complex from pea (Pisum sativum) was crystallized from ammonium sulfate solution at pH 5.2 in space group P3(1)21. The x-ray crystal structure was determined to 2.6-A resolution by multiple isomorphous replacement techniques. The structure was refined to an R value of 23% for reflections between 15- and 2.6-A resolution (F > 2 sigma), including the lipoate moiety and 50 water molecules, for the two protein molecules of the asymmetric unit. The 131-amino acid residues form seven beta-strands arranged into two antiparallel beta-sheets forming a "sandwich" structure. One alpha-helix is observed at the C-terminal end. The lipoate cofactor attached to Lys-63 is located in the loop of a hairpin configuration. The lipoate moiety points toward the residues His-34 and Asp-128 and is situated at the surface of the H-protein. This allows the flexibility of the lipoate arm. This is the first x-ray determination of a lipoic acid-containing protein, and the present results are in agreement with previous theoretical predictions and NMR studies of the catalytic domains of lipoic acid- and biotin-containing proteins.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/8197146-1354363,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8197146-1530594,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8197146-16667785,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8197146-1856858,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8197146-1888719,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8197146-1898363,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8197146-2025413,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8197146-3042770,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8197146-3143355,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8197146-3297708,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8197146-3522581,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8197146-4389630,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8197146-4585091,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8197146-5901047,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8197146-8357858,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8197146-8445635,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8197146-8518734
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
24
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pubmed:volume |
91
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4850-3
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pubmed:dateRevised |
2010-9-14
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pubmed:meshHeading |
pubmed-meshheading:8197146-Amino Acid Oxidoreductases,
pubmed-meshheading:8197146-Amino Acid Sequence,
pubmed-meshheading:8197146-Animals,
pubmed-meshheading:8197146-Carrier Proteins,
pubmed-meshheading:8197146-Crystallography, X-Ray,
pubmed-meshheading:8197146-Fabaceae,
pubmed-meshheading:8197146-Glycine Decarboxylase Complex,
pubmed-meshheading:8197146-Glycine Decarboxylase Complex H-Protein,
pubmed-meshheading:8197146-Glycine Dehydrogenase (Decarboxylating),
pubmed-meshheading:8197146-Humans,
pubmed-meshheading:8197146-Molecular Sequence Data,
pubmed-meshheading:8197146-Plants, Medicinal,
pubmed-meshheading:8197146-Protein Conformation,
pubmed-meshheading:8197146-Sequence Homology, Amino Acid,
pubmed-meshheading:8197146-Thioctic Acid
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pubmed:year |
1994
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pubmed:articleTitle |
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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pubmed:affiliation |
Institut de Biologie Structurale, Centre National de la Recherche Scientifique et Commissariat à l'Energie Atomique, Grenoble, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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