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1ltv

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[[Image:1ltv.jpg|left|200px]]<br /><applet load="1ltv" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ltv, resolution 2.00&Aring;" />
 
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'''CRYSTAL STRUCTURE OF CHROMOBACTERIUM VIOLACEUM PHENYLALANINE HYDROXYLASE, STRUCTURE WITH BOUND OXIDIZED Fe(III)'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF CHROMOBACTERIUM VIOLACEUM PHENYLALANINE HYDROXYLASE, STRUCTURE WITH BOUND OXIDIZED Fe(III)==
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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.
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<StructureSection load='1ltv' size='340' side='right'caption='[[1ltv]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ltv]] 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=1LTV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LTV FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
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<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></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ltv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ltv OCA], [https://pdbe.org/1ltv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ltv RCSB], [https://www.ebi.ac.uk/pdbsum/1ltv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ltv ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PH4H_CHRVO PH4H_CHRVO]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lt/1ltv_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1ltv ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1LTV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Chromobacterium_violaceum Chromobacterium violaceum] with <scene name='pdbligand=FE:'>FE</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Phenylalanine_4-monooxygenase Phenylalanine 4-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.16.1 1.14.16.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LTV OCA].
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*[[Hydroxylases 3D structures|Hydroxylases 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12096915 12096915]
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[[Category: Chromobacterium violaceum]]
[[Category: Chromobacterium violaceum]]
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[[Category: Phenylalanine 4-monooxygenase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Abu-Omar MM]]
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[[Category: Abu-Omar, M M.]]
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[[Category: Erlandsen H]]
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[[Category: Erlandsen, H.]]
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[[Category: Han A]]
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[[Category: Han, A.]]
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[[Category: Kim JY]]
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[[Category: Kim, J Y.]]
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[[Category: Patch MG]]
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[[Category: Patch, M G.]]
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[[Category: Stevens RC]]
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[[Category: Stevens, R C.]]
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[[Category: Volner A]]
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[[Category: Volner, A.]]
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[[Category: FE]]
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[[Category: catalytic core]]
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[[Category: iron-bound]]
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[[Category: phenylalanine hydroxylase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:48:25 2008''
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Current revision

CRYSTAL STRUCTURE OF CHROMOBACTERIUM VIOLACEUM PHENYLALANINE HYDROXYLASE, STRUCTURE WITH BOUND OXIDIZED Fe(III)

PDB ID 1ltv

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