1pxc

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[[Image:1pxc.gif|left|200px]]
 
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==CRYSTAL STRUCTURES OF MUTANT PSEUDOMONAS AERUGINOSA P-HYDROXYBENZOATE HYDROXYLASE: THE TYR201PHE, TYR385PHE, AND ASN300ASP VARIANTS==
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The line below this paragraph, containing "STRUCTURE_1pxc", creates the "Structure Box" on the page.
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<StructureSection load='1pxc' size='340' side='right'caption='[[1pxc]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1pxc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PXC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PXC FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.1&#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=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=PHB:P-HYDROXYBENZOIC+ACID'>PHB</scene></td></tr>
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{{STRUCTURE_1pxc| PDB=1pxc | SCENE= }}
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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=1pxc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pxc OCA], [https://pdbe.org/1pxc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pxc RCSB], [https://www.ebi.ac.uk/pdbsum/1pxc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pxc ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PHHY_PSEAE PHHY_PSEAE]
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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/px/1pxc_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=1pxc ConSurf].
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<div style="clear:both"></div>
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'''CRYSTAL STRUCTURES OF MUTANT PSEUDOMONAS AERUGINOSA P-HYDROXYBENZOATE HYDROXYLASE: THE TYR201PHE, TYR385PHE, AND ASN300ASP VARIANTS'''
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==See Also==
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*[[Hydroxylases 3D structures|Hydroxylases 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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Structures of the mutant p-hydroxybenzoate hydroxylases, Tyr201Phe, Tyr385Phe, and Asn300Asp, each complexed with the substrate p-OHB have been determined by X-ray crystallography. Crystals of these three mutants of the Pseudomonas aeruginosa enzyme, which differs from the wild-type Pseudomonas fluorescens enzyme at two surface positions (228 and 249), were isomorphous with crystals of the wild-type P. fluorescens enzyme, allowing the mutant structures to be determined by model building and refinement, starting from the coordinates for the oxidized P. fluorescens PHBH-3,4-diOHB complex [Schreuder, H.A., van der Laan, J.M., Hol, W.G.J., &amp; Drenth, J. (1988) J. Mol. Biol. 199, 637-648]. The R factors for the structures described here are: Tyr385Phe, 0.178 for data from 40.0 to 2.1 A; Tyr201Phe, 0.203 for data from 40.0 to 2.3 A; and Asn300Asp, 0.193 for data from 40.0 to 2.3 A. The functional effects of the Tyr201Phe and Tyr385Phe mutations, described earlier [Entsch, B., Palfey, B.A., Ballou, D.P., &amp; Massey, V. (1991) J. Biol. Chem. 266, 17341-17349], were rationalized with the assumption that the mutations perturbed the hydrogen-bonding interactions of the tyrosine residues but caused no other changes in the enzyme structure. In agreement with these assumptions, the positions of the substrate, the flavin, and the modified residues are not altered in the Tyr385Phe and Tyr201Phe structures. In contrast, substitution of Asp for Asn at residue 300 has more profound effects on the enzyme structure. The side chain of Asp300 moves away from the flavin, disrupting the interactions of the carboxamide group with the flavin O(2) atom, and the alpha-helix H10 that begins at residue 297 is displaced, altering its dipole interactions with the flavin ring. The functional consequences of these changes in the enzyme structure and of the introduction of the carboxyl group at 300 are described and discussed in the accompanying paper (Palfey et al., 1994b).
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[[Category: Large Structures]]
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==About this Structure==
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1PXC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PXC OCA].
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==Reference==
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Crystal structures of mutant Pseudomonas aeruginosa p-hydroxybenzoate hydroxylases: the Tyr201Phe, Tyr385Phe, and Asn300Asp variants., Lah MS, Palfey BA, Schreuder HA, Ludwig ML, Biochemistry. 1994 Feb 15;33(6):1555-64. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8312276 8312276]
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[[Category: 4-hydroxybenzoate 3-monooxygenase]]
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[[Category: Pseudomonas aeruginosa]]
[[Category: Pseudomonas aeruginosa]]
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[[Category: Single protein]]
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[[Category: Lah MS]]
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[[Category: Lah, M S.]]
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[[Category: Ludwig ML]]
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[[Category: Ludwig, M L.]]
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[[Category: Palfey BA]]
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[[Category: Palfey, B A.]]
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[[Category: Schreuder HA]]
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[[Category: Schreuder, H A.]]
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[[Category: Oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:35:50 2008''
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Current revision

CRYSTAL STRUCTURES OF MUTANT PSEUDOMONAS AERUGINOSA P-HYDROXYBENZOATE HYDROXYLASE: THE TYR201PHE, TYR385PHE, AND ASN300ASP VARIANTS

PDB ID 1pxc

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