3tk2: Difference between revisions
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==Crystallographic structure of phenylalanine hydroxylase from Chromobacterium violaceum cocrystallized with phenylalanine in a site distal to the active site== | ==Crystallographic structure of phenylalanine hydroxylase from Chromobacterium violaceum cocrystallized with phenylalanine in a site distal to the active site== | ||
<StructureSection load='3tk2' size='340' side='right' caption='[[3tk2]], [[Resolution|resolution]] 1.35Å' scene=''> | <StructureSection load='3tk2' size='340' side='right'caption='[[3tk2]], [[Resolution|resolution]] 1.35Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3tk2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3tk2]] is a 1 chain structure with sequence from [http://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=3TK2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TK2 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=PHE:PHENYLALANINE'>PHE</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=PHE:PHENYLALANINE'>PHE</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3tcy|3tcy]], [[3tk4|3tk4]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3tcy|3tcy]], [[3tk4|3tk4]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">phhA, CV_3180 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=536 Chromobacterium | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">phhA, CV_3180 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=536 "Chromobacterium janthinum" (Zopf) Ford 1927])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3tk2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tk2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3tk2 RCSB], [http://www.ebi.ac.uk/pdbsum/3tk2 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3tk2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tk2 OCA], [http://pdbe.org/3tk2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3tk2 RCSB], [http://www.ebi.ac.uk/pdbsum/3tk2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3tk2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3tk2" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[ | *[[Hydroxylases 3D structures|Hydroxylases 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Phenylalanine 4-monooxygenase]] | [[Category: Phenylalanine 4-monooxygenase]] | ||
[[Category: Abu-Omar, M M]] | [[Category: Abu-Omar, M M]] | ||
Revision as of 18:53, 20 November 2019
Crystallographic structure of phenylalanine hydroxylase from Chromobacterium violaceum cocrystallized with phenylalanine in a site distal to the active siteCrystallographic structure of phenylalanine hydroxylase from Chromobacterium violaceum cocrystallized with phenylalanine in a site distal to the active site
Structural highlights
Publication Abstract from PubMedPhenylalanine hydroxylase (PAH) is a non-heme iron enzyme that catalyzes oxidation of phenylalanine to tyrosine, a reaction that must be kept under tight regulatory control. Mammalian PAH has a regulatory domain in which binding of the substrate leads to allosteric activation of the enzyme. However, the existence of PAH regulation in evolutionarily distant organisms, for example some bacteria in which it occurs, has so far been underappreciated. In an attempt to crystallographically characterize substrate binding by PAH from Chromobacterium violaceum, a single-domain monomeric enzyme, electron density for phenylalanine was observed at a distal site 15.7 A from the active site. Isothermal titration calorimetry (ITC) experiments revealed a dissociation constant of 24 +/- 1.1 muM for phenylalanine. Under the same conditions, ITC revealed no detectable binding for alanine, tyrosine, or isoleucine, indicating the distal site may be selective for phenylalanine. Point mutations of amino acid residues in the distal site that contact phenylalanine (F258A, Y155A, T254A) led to impaired binding, consistent with the presence of distal site binding in solution. Although kinetic analysis revealed that the distal site mutants suffer discernible loss of their catalytic activity, X-ray crystallographic analysis of Y155A and F258A, the two mutants with the most noticeable decrease in activity, revealed no discernible change in the structure of their active sites, suggesting that the effect of distal binding may result from protein dynamics in solution. An additional substrate binding site in a bacterial phenylalanine hydroxylase.,Ronau JA, Paul LN, Fuchs JE, Corn IR, Wagner KT, Liedl KR, Abu-Omar MM, Das C Eur Biophys J. 2013 Jul 17. PMID:23860686[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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