1bw9
From Proteopedia
(New page: 200px<br /><applet load="1bw9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bw9, resolution 1.5Å" /> '''PHENYLALANINE DEHYDRO...) |
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| - | [[Image:1bw9.gif|left|200px]]<br /><applet load="1bw9" size=" | + | [[Image:1bw9.gif|left|200px]]<br /><applet load="1bw9" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1bw9, resolution 1.5Å" /> | caption="1bw9, resolution 1.5Å" /> | ||
'''PHENYLALANINE DEHYDROGENASE STRUCTURE IN TERNARY COMPLEX WITH NAD+ AND PHENYLPYRUVATE'''<br /> | '''PHENYLALANINE DEHYDROGENASE STRUCTURE IN TERNARY COMPLEX WITH NAD+ AND PHENYLPYRUVATE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The molecular structures of recombinant L-phenylalanine dehydrogenase from | + | 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== | ==About this Structure== | ||
| - | 1BW9 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, NA, PO4, NAD, PPY, EDO and IPA 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:// | + | 1BW9 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 <scene name='pdbligand=K:'>K</scene>, <scene name='pdbligand=NA:'>NA</scene>, <scene name='pdbligand=PO4:'>PO4</scene>, <scene name='pdbligand=NAD:'>NAD</scene>, <scene name='pdbligand=PPY:'>PPY</scene>, <scene name='pdbligand=EDO:'>EDO</scene> and <scene name='pdbligand=IPA:'>IPA</scene> 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1BW9 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Rhodococcus sp.]] | [[Category: Rhodococcus sp.]] | ||
| - | [[Category: Blanchard, J | + | [[Category: Blanchard, J L.]] |
| - | [[Category: Brunhuber, N | + | [[Category: Brunhuber, N M.W.]] |
| - | [[Category: Holden, H | + | [[Category: Holden, H M.]] |
| - | [[Category: Thoden, J | + | [[Category: Thoden, J B.]] |
| - | [[Category: Vanhooke, J | + | [[Category: Vanhooke, J L.]] |
[[Category: EDO]] | [[Category: EDO]] | ||
[[Category: IPA]] | [[Category: IPA]] | ||
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[[Category: oxidative deamination mechanism]] | [[Category: oxidative deamination mechanism]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:59:46 2008'' |
Revision as of 09:59, 21 February 2008
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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. with , , , , , and as ligands. Active as Phenylalanine dehydrogenase, with EC number 1.4.1.20 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
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