1mlw
From Proteopedia
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'''Crystal structure of human tryptophan hydroxylase with bound 7,8-dihydro-L-biopterin cofactor and Fe(III)''' | '''Crystal structure of human tryptophan hydroxylase with bound 7,8-dihydro-L-biopterin cofactor and Fe(III)''' | ||
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[[Category: Stevens, R C.]] | [[Category: Stevens, R C.]] | ||
[[Category: Wang, L.]] | [[Category: Wang, L.]] | ||
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Revision as of 22:23, 2 May 2008
Crystal structure of human tryptophan hydroxylase with bound 7,8-dihydro-L-biopterin cofactor and Fe(III)
Overview
Tryptophan hydroxylase oxidizes L-tryptophan to 5-hydroxy-L-tryptophan in the rate-determining step of serotonin biosynthesis. We have determined the X-ray crystal structure (1.7 A) of a truncated functional form of human tryptophan hydroxylase with the bound cofactor analogue 7,8-dihydro-L-biopterin, providing the first atomic-resolution information for the catalytic domain of this important enzyme. Comparison of the three-dimensional structures of all three members of the aromatic amino acid hydroxylase family--tyrosine hydroxylase, phenylalanine hydroxylase, and tryptophan hydroxylase--reveals important differences at the active sites.
About this Structure
1MLW is a Single protein structure of sequence from Homo sapiens. The following page contains interesting information on the relation of 1MLW with [Phenylalanine Hydroxylase]. Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of human tryptophan hydroxylase and its implications for the biosynthesis of the neurotransmitters serotonin and melatonin., Wang L, Erlandsen H, Haavik J, Knappskog PM, Stevens RC, Biochemistry. 2002 Oct 22;41(42):12569-74. PMID:12379098 Page seeded by OCA on Sat May 3 01:23:52 2008
