2g25: Difference between revisions
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[[Image:2g25.gif|left|200px]] | [[Image:2g25.gif|left|200px]] | ||
'''E. Coli Pyruvate Dehydrogenase Phosphonolactylthiamin Diphosphate Complex''' | {{Structure | ||
|PDB= 2g25 |SIZE=350|CAPTION= <scene name='initialview01'>2g25</scene>, resolution 2.10Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> and <scene name='pdbligand=TDK:3-[(4-AMINO-2-METHYLPYRIMIDIN-5-YL)METHYL]-2-{(1S)-1-HYDROXY-1-[(R)-HYDROXY(METHOXY)PHOSPHORYL]ETHYL}-5-(2-{[(S)-HYDROXY(PHOSPHONOOXY)PHOSPHORYL]OXY}ETHYL)-4-METHYL-1,3-THIAZOL-3-IUM'>TDK</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Pyruvate_dehydrogenase_(acetyl-transferring) Pyruvate dehydrogenase (acetyl-transferring)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.4.1 1.2.4.1] | |||
|GENE= aceE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |||
}} | |||
'''E. Coli Pyruvate Dehydrogenase Phosphonolactylthiamin Diphosphate Complex''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2G25 is a [ | 2G25 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G25 OCA]. | ||
==Reference== | ==Reference== | ||
A thiamin-bound, pre-decarboxylation reaction intermediate analogue in the pyruvate dehydrogenase E1 subunit induces large scale disorder-to-order transformations in the enzyme and reveals novel structural features in the covalently bound adduct., Arjunan P, Sax M, Brunskill A, Chandrasekhar K, Nemeria N, Zhang S, Jordan F, Furey W, J Biol Chem. 2006 Jun 2;281(22):15296-303. Epub 2006 Mar 10. PMID:[http:// | A thiamin-bound, pre-decarboxylation reaction intermediate analogue in the pyruvate dehydrogenase E1 subunit induces large scale disorder-to-order transformations in the enzyme and reveals novel structural features in the covalently bound adduct., Arjunan P, Sax M, Brunskill A, Chandrasekhar K, Nemeria N, Zhang S, Jordan F, Furey W, J Biol Chem. 2006 Jun 2;281(22):15296-303. Epub 2006 Mar 10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16531404 16531404] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Pyruvate dehydrogenase (acetyl-transferring)]] | [[Category: Pyruvate dehydrogenase (acetyl-transferring)]] | ||
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[[Category: pyruvate dehydrogenase e1 component]] | [[Category: pyruvate dehydrogenase e1 component]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:59:32 2008'' | ||