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    Nature. 1977 Mar 24;266(5600):328-33.

    Sequence and structure of D-glyceraldehyde 3-phosphate dehydrogenase from Bacillus stearothermophilus.

    Biesecker G, Harris JI, Thierry JC, Walker JE, Wonacott AJ.

    The glyceraldehyde 3-phosphate dehydogenase holoenzyme of Bacillus stearothermophilus possesses precise 222 symmetry: in this respect it differs from the reported structure of the lobster muscle enzyme. Pairs of active sites are linked through a flexible polypeptide loop which probably mediates the structural changes giving rise to cooperative effects. Three additional salt bridges made by each subunit to others would make a major contribution to thermostability of the tetramer.

    PMID: 193030 [PubMed - indexed for MEDLINE]

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