1mlw
From Proteopedia
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|PDB= 1mlw |SIZE=350|CAPTION= <scene name='initialview01'>1mlw</scene>, resolution 1.71Å | |PDB= 1mlw |SIZE=350|CAPTION= <scene name='initialview01'>1mlw</scene>, resolution 1.71Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene> | + | |LIGAND= <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=HBI:7,8-DIHYDROBIOPTERIN'>HBI</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Tryptophan_5-monooxygenase Tryptophan 5-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.16.4 1.14.16.4] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Tryptophan_5-monooxygenase Tryptophan 5-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.16.4 1.14.16.4] </span> |
|GENE= TPH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= TPH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mlw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mlw OCA], [http://www.ebi.ac.uk/pdbsum/1mlw PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mlw RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==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. | 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. | ||
| - | |||
| - | ==Disease== | ||
| - | Known disease associated with this structure: Unipolar depression, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=607478 607478]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Stevens, R C.]] | [[Category: Stevens, R C.]] | ||
[[Category: Wang, L.]] | [[Category: Wang, L.]] | ||
| - | [[Category: FE]] | ||
| - | [[Category: HBI]] | ||
[[Category: aromatic amino acid hydroxylase catalytic domain fold]] | [[Category: aromatic amino acid hydroxylase catalytic domain fold]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:17:48 2008'' |
Revision as of 19:17, 30 March 2008
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| , resolution 1.71Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | TPH (Homo sapiens) | ||||||
| Activity: | Tryptophan 5-monooxygenase, with EC number 1.14.16.4 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Sun Mar 30 22:17:48 2008
