1mlw: Difference between revisions

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New page: left|200px<br /> <applet load="1mlw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mlw, resolution 1.71Å" /> '''Crystal structure o...
 
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[[Image:1mlw.gif|left|200px]]<br />
[[Image:1mlw.gif|left|200px]]<br /><applet load="1mlw" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1mlw" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1mlw, resolution 1.71&Aring;" />
caption="1mlw, resolution 1.71&Aring;" />
'''Crystal structure of human tryptophan hydroxylase with bound 7,8-dihydro-L-biopterin cofactor and Fe(III)'''<br />
'''Crystal structure of human tryptophan hydroxylase with bound 7,8-dihydro-L-biopterin cofactor and Fe(III)'''<br />


==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==
==Disease==
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==About this Structure==
==About this Structure==
1MLW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with FE and HBI as [http://en.wikipedia.org/wiki/ligands ligands]. The following page contains interesting information on the relation of 1MLW with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb61_1.html Phenylalanine Hydroxylase]]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MLW OCA].  
1MLW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=FE:'>FE</scene> and <scene name='pdbligand=HBI:'>HBI</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. The following page contains interesting information on the relation of 1MLW with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb61_1.html Phenylalanine Hydroxylase]]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MLW OCA].  


==Reference==
==Reference==
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[[Category: Erlandsen, H.]]
[[Category: Erlandsen, H.]]
[[Category: Haavik, J.]]
[[Category: Haavik, J.]]
[[Category: Knappskog, P.M.]]
[[Category: Knappskog, P M.]]
[[Category: Stevens, R.C.]]
[[Category: Stevens, R C.]]
[[Category: Wang, L.]]
[[Category: Wang, L.]]
[[Category: FE]]
[[Category: FE]]
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[[Category: aromatic amino acid hydroxylase catalytic domain fold]]
[[Category: aromatic amino acid hydroxylase catalytic domain fold]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:12:55 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:56:32 2008''