1bw9

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[[Image:1bw9.gif|left|200px]]
[[Image:1bw9.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1bw9 |SIZE=350|CAPTION= <scene name='initialview01'>1bw9</scene>, resolution 1.5&Aring;
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The line below this paragraph, containing "STRUCTURE_1bw9", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=PPY:3-PHENYLPYRUVIC+ACID'>PPY</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1bw9| PDB=1bw9 | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bw9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bw9 OCA], [http://www.ebi.ac.uk/pdbsum/1bw9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bw9 RCSB]</span>
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}}
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'''PHENYLALANINE DEHYDROGENASE STRUCTURE IN TERNARY COMPLEX WITH NAD+ AND PHENYLPYRUVATE'''
'''PHENYLALANINE DEHYDROGENASE STRUCTURE IN TERNARY COMPLEX WITH NAD+ AND PHENYLPYRUVATE'''
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[[Category: Thoden, J B.]]
[[Category: Thoden, J B.]]
[[Category: Vanhooke, J L.]]
[[Category: Vanhooke, J L.]]
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[[Category: amino acid dehydrogenase]]
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[[Category: Amino acid dehydrogenase]]
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[[Category: oxidative deamination mechanism]]
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[[Category: Oxidative deamination mechanism]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:01:50 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:09:32 2008''
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Revision as of 09:01, 2 May 2008

Image:1bw9.gif

Template:STRUCTURE 1bw9

PHENYLALANINE DEHYDROGENASE STRUCTURE IN TERNARY COMPLEX WITH NAD+ AND PHENYLPYRUVATE


Overview

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.

About this Structure

1BW9 is a Protein complex structure of sequences from Rhodococcus sp.. Full crystallographic information is available from OCA.

Reference

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:10029526 Page seeded by OCA on Fri May 2 12:01:50 2008

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