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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 />
<applet load="1mlw" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1mlw, resolution 1.71&Aring;" />
'''Crystal structure of human tryptophan hydroxylase with bound 7,8-dihydro-L-biopterin cofactor and Fe(III)'''<br />


==Overview==
==Crystal structure of human tryptophan hydroxylase with bound 7,8-dihydro-L-biopterin cofactor and Fe(III)==
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.
<StructureSection load='1mlw' size='340' side='right'caption='[[1mlw]], [[Resolution|resolution]] 1.71&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1mlw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. The January 2005 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Phenylalanine Hydroxylase''  by Shuchismita Dutta and David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2005_1 10.2210/rcsb_pdb/mom_2005_1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MLW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MLW FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.71&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=HBI:7,8-DIHYDROBIOPTERIN'>HBI</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mlw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mlw OCA], [https://pdbe.org/1mlw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mlw RCSB], [https://www.ebi.ac.uk/pdbsum/1mlw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mlw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TPH1_HUMAN TPH1_HUMAN]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ml/1mlw_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1mlw ConSurf].
<div style="clear:both"></div>


==Disease==
==See Also==
Known disease associated with this structure: Unipolar depression, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=607478 607478]]
*[[Hydroxylases 3D structures|Hydroxylases 3D structures]]
 
*[[Monooxygenase 3D structures|Monooxygenase 3D structures]]
==About this Structure==
__TOC__
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].
</StructureSection>
 
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12379098 12379098]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Phenylalanine Hydroxylase]]
[[Category: Phenylalanine Hydroxylase]]
[[Category: Single protein]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: Tryptophan 5-monooxygenase]]
[[Category: Erlandsen H]]
[[Category: Erlandsen, H.]]
[[Category: Haavik J]]
[[Category: Haavik, J.]]
[[Category: Knappskog PM]]
[[Category: Knappskog, P.M.]]
[[Category: Stevens RC]]
[[Category: Stevens, R.C.]]
[[Category: Wang L]]
[[Category: Wang, L.]]
[[Category: FE]]
[[Category: HBI]]
[[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''

Latest revision as of 07:45, 14 February 2024

Crystal structure of human tryptophan hydroxylase with bound 7,8-dihydro-L-biopterin cofactor and Fe(III)

1mlw, resolution 1.71Å

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