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<StructureSection load='1ltu' size='340' side='right'caption='[[1ltu]], [[Resolution|resolution]] 1.74&Aring;' scene=''>
<StructureSection load='1ltu' size='340' side='right'caption='[[1ltu]], [[Resolution|resolution]] 1.74&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1ltu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"chromobacterium_janthinum"_(zopf)_ford_1927 "chromobacterium janthinum" (zopf) ford 1927]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LTU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LTU FirstGlance]. <br>
<table><tr><td colspan='2'>[[1ltu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Chromobacterium_violaceum Chromobacterium violaceum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LTU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LTU FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ltv|1ltv]], [[1ltz|1ltz]]</div></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.74&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Phenylalanine_4-monooxygenase Phenylalanine 4-monooxygenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.16.1 1.14.16.1] </span></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=1ltu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ltu OCA], [https://pdbe.org/1ltu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ltu RCSB], [https://www.ebi.ac.uk/pdbsum/1ltu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ltu ProSAT]</span></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=1ltu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ltu OCA], [https://pdbe.org/1ltu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ltu RCSB], [https://www.ebi.ac.uk/pdbsum/1ltu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ltu ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PH4H_CHRVO PH4H_CHRVO]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1ltu ConSurf].
</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=1ltu ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Structure determination of bacterial homologues of human disease-related proteins provides an efficient path to understanding the three-dimensional fold of proteins that are associated with human diseases. However, the precise locations of active-site residues are often quite different between bacterial and human versions of an enzyme, creating significant differences in the biological understanding of enzyme homologs. To study this hypothesis, phenylalanine hydroxylase from a bacterial source has been structurally characterized at high resolution and comparison is made to the human analog. The enzyme phenylalanine hydroxylase (PheOH) catalyzes the hydroxylation of l-phenylalanine into l-tyrosine utilizing the cofactors (6R)-l-erythro-5,6,7,8 tetrahydrobiopterin (BH(4)) and molecular oxygen. Previously determined X-ray structures of human and rat PheOH, with a sequence identity of more than 93%, show that these two structures are practically identical. It is thus of interest to compare the structure of the divergent Chromobacterium violaceum phenylalanine hydroxylase (CvPheOH) ( approximately 24% sequence identity overall) to the related human and rat PheOH structures. We have determined crystal structures of CvPheOH to high resolution in the apo-form (no Fe-added), Fe(III)-bound form, and 7,8-dihydro-l-biopterin (7,8-BH(2)) plus Fe(III)-bound form. The bacterial enzyme displays higher activity and thermal melting temperature, and structurally, differences are observed in the N and C termini, and in a loop close to the active-site iron atom.
Structural comparison of bacterial and human iron-dependent phenylalanine hydroxylases: similar fold, different stability and reaction rates.,Erlandsen H, Kim JY, Patch MG, Han A, Volner A, Abu-Omar MM, Stevens RC J Mol Biol. 2002 Jul 12;320(3):645-61. PMID:12096915<ref>PMID:12096915</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1ltu" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Hydroxylases 3D structures|Hydroxylases 3D structures]]
*[[Hydroxylases 3D structures|Hydroxylases 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Chromobacterium violaceum]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Phenylalanine 4-monooxygenase]]
[[Category: Abu-Omar MM]]
[[Category: Abu-Omar, M M]]
[[Category: Erlandsen H]]
[[Category: Erlandsen, H]]
[[Category: Han A]]
[[Category: Han, A]]
[[Category: Kim JY]]
[[Category: Kim, J Y]]
[[Category: Patch MG]]
[[Category: Patch, M G]]
[[Category: Stevens RC]]
[[Category: Stevens, R C]]
[[Category: Volner A]]
[[Category: Volner, A]]
[[Category: Oxidoreductase]]
[[Category: Phenylalanine hydroxylase apo-structure]]
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