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1bxg

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(New page: 200px<br /><applet load="1bxg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bxg, resolution 2.3&Aring;" /> '''PHENYLALANINE DEHYDRO...)
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[[Image:1bxg.jpg|left|200px]]<br /><applet load="1bxg" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1bxg, resolution 2.3&Aring;" />
 
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'''PHENYLALANINE DEHYDROGENASE STRUCTURE IN TERNARY COMPLEX WITH NAD+ AND BETA-PHENYLPROPIONATE'''<br />
 
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==Overview==
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==PHENYLALANINE DEHYDROGENASE STRUCTURE IN TERNARY COMPLEX WITH NAD+ AND BETA-PHENYLPROPIONATE==
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The molecular structures of recombinant L-phenylalanine dehydrogenase from, Rhodococcus sp. M4 in two different inhibitory ternary complexes have been, determined by X-ray crystallographic analyses to high resolution. Both, structures show that L-phenylalanine dehydrogenase is a homodimeric enzyme, with each monomer composed of distinct globular N- and C-terminal domains, separated by a deep cleft containing the active site. The N-terminal, domain binds the amino acid substrate and contributes to the interactions, at the subunit:subunit interface. The C-terminal domain contains a typical, Rossmann fold and orients the dinucleotide. The dimer has overall, dimensions of approximately 82 A x 75 A x 75 A, with roughly 50 A, separating the two active sites. The structures described here, namely the, enzyme.NAD+.phenylpyruvate, and enzyme. NAD+.beta-phenylpropionate, species, represent the first models for any amino acid dehydrogenase in a, ternary complex. By analysis of the active-site interactions in these, models, along with the currently available kinetic data, a detailed, chemical mechanism has been proposed. This mechanism differs from those, proposed to date in that it accounts for the inability of the amino acid, dehydrogenases, in general, to function as hydroxy acid dehydrogenases.
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<StructureSection load='1bxg' size='340' side='right'caption='[[1bxg]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1bxg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodococcus_sp. Rhodococcus sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BXG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BXG FirstGlance]. <br>
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1BXG is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rhodococcus_sp. Rhodococcus sp.] with K, PO4, NAD and HCI as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Phenylalanine_dehydrogenase Phenylalanine dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.1.20 1.4.1.20] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BXG OCA].
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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]] 2.3&#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=HCI:HYDROCINNAMIC+ACID'>HCI</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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==Reference==
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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=1bxg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bxg OCA], [https://pdbe.org/1bxg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bxg RCSB], [https://www.ebi.ac.uk/pdbsum/1bxg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bxg ProSAT]</span></td></tr>
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Phenylalanine dehydrogenase from Rhodococcus sp. M4: high-resolution X-ray analyses of inhibitory ternary complexes reveal key features in the oxidative deamination mechanism., Vanhooke JL, Thoden JB, Brunhuber NM, Blanchard JS, Holden HM, Biochemistry. 1999 Feb 23;38(8):2326-39. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10029526 10029526]
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</table>
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[[Category: Phenylalanine dehydrogenase]]
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== Function ==
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[[Category: Protein complex]]
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[https://www.uniprot.org/uniprot/DHPH_RHOSO DHPH_RHOSO] Catalyzes the reversible NAD(+)-dependent oxidative deamination of L-phenylalanine to phenylpyruvate.<ref>PMID:10924111</ref> <ref>PMID:8206922</ref>
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[[Category: Rhodococcus sp.]]
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== Evolutionary Conservation ==
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[[Category: Blanchard, J.L.]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: Brunhuber, N.M.W.]]
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Check<jmol>
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[[Category: Holden, H.M.]]
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<jmolCheckbox>
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[[Category: Thoden, J.B.]]
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bx/1bxg_consurf.spt"</scriptWhenChecked>
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[[Category: Vanhooke, J.L.]]
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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[[Category: HCI]]
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<text>to colour the structure by Evolutionary Conservation</text>
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[[Category: K]]
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</jmolCheckbox>
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[[Category: NAD]]
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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=1bxg ConSurf].
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[[Category: PO4]]
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<div style="clear:both"></div>
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[[Category: amino acid dehydrogenase]]
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== References ==
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[[Category: oxidative deamination mechanism]]
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<references/>
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__TOC__
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 00:45:05 2007''
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Rhodococcus sp]]
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[[Category: Blanchard JL]]
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[[Category: Brunhuber NMW]]
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[[Category: Holden HM]]
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[[Category: Thoden JB]]
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[[Category: Vanhooke JL]]

Current revision

PHENYLALANINE DEHYDROGENASE STRUCTURE IN TERNARY COMPLEX WITH NAD+ AND BETA-PHENYLPROPIONATE

PDB ID 1bxg

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