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Accession number;06A0759483
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| Title;Crystal Structure of Glycine Cleavage System P-protein Provides Insights into the Molecular Basis of Hyperglycinemia |
| Author;
NAKAI TADASHI
(Inst. of Physical and Chemical Res.)
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Journal Title;Journal of the Crystallographic Society of Japan
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Journal Code:G0232A
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ISSN:0369-4585
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VOL.48;NO.4;PAGE.265-270(2006)
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| Figure&Table&Reference;FIG.7, TBL.2, REF.16 |
| Pub. Country;Japan |
| Language;Japanese |
| Abstract;The crystal structure of the P-protein of the glycine cleavage system from Thermus thermophilus HB8 has been determined, which reveals that P-proteins do not involve the .ALPHA.2 dimer universally observed in the evolutionarily related pyridoxal 5'-phosphate (PLP)-dependent enzymes. Instead, novel .ALPHA..BETA. dimers associate to form an .ALPHA.2.BETA.2 tetramer. The crystal structure of P-protein without PLP has also been analyzed. These structures allow the identification of functionally important residues involved in recognition of the cofactor and substrates, and show that most of these residues are well conserved among all living organisms. These results provide insights into the molecular basis of hyperglycinemia. (author abst.) |
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