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1cjx
From Proteopedia
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Revision as of 12:54, 30 October 2007
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CRYSTAL STRUCTURE OF PSEUDOMONAS FLUORESCENS HPPD
Overview
BACKGROUND: In plants and photosynthetic bacteria, the tyrosine, degradation pathway is crucial because homogentisate, a tyrosine, degradation product, is a precursor for the biosynthesis of photosynthetic, pigments, such as quinones or tocophenols. Homogentisate biosynthesis, includes a decarboxylation step, a dioxygenation and a rearrangement of, the pyruvate sidechain. This complex reaction is carried out by a single, enzyme, the 4-hydroxyphenylpyruvate dioxygenase (HPPD), a non-heme iron, dependent enzyme that is active as a homotetramer in bacteria and as a, homodimer in plants. Moreover, in humans, a HPPD deficiency is found to be, related to tyrosinemia, a rare hereditary disorder of tyrosine catabolism., RESULTS: We report here the crystal structure of Pseudomonas fluorescens, ... [(full description)]
About this Structure
1CJX is a [Single protein] structure of sequence from [Pseudomonas fluorescens] with FE2, EMC and ACT as [ligands]. Active as [4-hydroxyphenylpyruvate dioxygenase], with EC number [1.13.11.27]. Structure known Active Sites: ASA, ASB, ASC and ASD. Full crystallographic information is available from [OCA].
Reference
Crystal structure of Pseudomonas fluorescens 4-hydroxyphenylpyruvate dioxygenase: an enzyme involved in the tyrosine degradation pathway., Serre L, Sailland A, Sy D, Boudec P, Rolland A, Pebay-Peyroula E, Cohen-Addad C, Structure. 1999 Aug 15;7(8):977-88. PMID:10467142
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