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New page: left|200px<br /><applet load="1dnl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dnl, resolution 1.8Å" /> '''X-RAY STRUCTURE OF ES...
 
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[[Image:1dnl.jpg|left|200px]]<br /><applet load="1dnl" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1dnl.jpg|left|200px]]<br /><applet load="1dnl" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1dnl, resolution 1.8&Aring;" />
caption="1dnl, resolution 1.8&Aring;" />
'''X-RAY STRUCTURE OF ESCHERICHIA COLI PYRIDOXINE 5'-PHOSPHATE OXIDASE COMPLEXED WITH FMN AT 1.8 ANGSTROM RESOLUTION'''<br />
'''X-RAY STRUCTURE OF ESCHERICHIA COLI PYRIDOXINE 5'-PHOSPHATE OXIDASE COMPLEXED WITH FMN AT 1.8 ANGSTROM RESOLUTION'''<br />


==Overview==
==Overview==
BACKGROUND: Escherichia coli pyridoxine 5'-phosphate oxidase (PNPOx), catalyzes the terminal step in the biosynthesis of pyridoxal 5'-phosphate, (PLP), a cofactor used by many enzymes involved in amino acid metabolism., The enzyme oxidizes either the 4'-hydroxyl group of pyridoxine, 5'-phosphate (PNP) or the 4'-primary amine of pyridoxamine 5'-phosphate, (PMP) to an aldehyde. PNPOx is a homodimeric enzyme with one flavin, mononucleotide (FMN) molecule non-covalently bound to each subunit. A high, degree of sequence homology among the 15 known members of the PNPOx family, suggests that all members of this group have similar three-dimensional, folds. RESULTS: The crystal structure of PNPOx from E. coli has been, determined to 1.8 A resolution. The monomeric subunit folds into an, eight-stranded beta sheet surrounded by five alpha-helical structures. Two, monomers related by a twofold axis interact extensively along one-half of, each monomer to form the dimer. There are two clefts at the dimer, interface that are symmetry-related and extend from the top to the bottom, of the dimer. An FMN cofactor that makes interactions with both subunits, is located in each of these two clefts. CONCLUSIONS: The structure is, quite similar to the recently deposited 2.7 A structure of Saccharomyces, cerevisiae PNPOx and also, remarkably, shares a common structural fold, with the FMN-binding protein from Desulfovibrio vulgaris and a domain of, chymotrypsin. This high-resolution E. coli PNPOx structure permits, predictions to be made about residues involved in substrate binding and, catalysis. These predictions provide testable hypotheses, which can be, answered by making site-directed mutants.
BACKGROUND: Escherichia coli pyridoxine 5'-phosphate oxidase (PNPOx) catalyzes the terminal step in the biosynthesis of pyridoxal 5'-phosphate (PLP), a cofactor used by many enzymes involved in amino acid metabolism. The enzyme oxidizes either the 4'-hydroxyl group of pyridoxine 5'-phosphate (PNP) or the 4'-primary amine of pyridoxamine 5'-phosphate (PMP) to an aldehyde. PNPOx is a homodimeric enzyme with one flavin mononucleotide (FMN) molecule non-covalently bound to each subunit. A high degree of sequence homology among the 15 known members of the PNPOx family suggests that all members of this group have similar three-dimensional folds. RESULTS: The crystal structure of PNPOx from E. coli has been determined to 1.8 A resolution. The monomeric subunit folds into an eight-stranded beta sheet surrounded by five alpha-helical structures. Two monomers related by a twofold axis interact extensively along one-half of each monomer to form the dimer. There are two clefts at the dimer interface that are symmetry-related and extend from the top to the bottom of the dimer. An FMN cofactor that makes interactions with both subunits is located in each of these two clefts. CONCLUSIONS: The structure is quite similar to the recently deposited 2.7 A structure of Saccharomyces cerevisiae PNPOx and also, remarkably, shares a common structural fold with the FMN-binding protein from Desulfovibrio vulgaris and a domain of chymotrypsin. This high-resolution E. coli PNPOx structure permits predictions to be made about residues involved in substrate binding and catalysis. These predictions provide testable hypotheses, which can be answered by making site-directed mutants.


==About this Structure==
==About this Structure==
1DNL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with PO4 and FMN as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Pyridoxal_5'-phosphate_synthase Pyridoxal 5'-phosphate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.5 1.4.3.5] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DNL OCA].  
1DNL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=PO4:'>PO4</scene> and <scene name='pdbligand=FMN:'>FMN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Pyridoxal_5'-phosphate_synthase Pyridoxal 5'-phosphate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.5 1.4.3.5] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DNL OCA].  


==Reference==
==Reference==
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[[Category: Pyridoxal 5'-phosphate synthase]]
[[Category: Pyridoxal 5'-phosphate synthase]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Abraham, D.J.]]
[[Category: Abraham, D J.]]
[[Category: Mathews, I.]]
[[Category: Mathews, I.]]
[[Category: Musayev, F.N.]]
[[Category: Musayev, F N.]]
[[Category: Safo, M.K.]]
[[Category: Safo, M K.]]
[[Category: Salvo, M.L.di.]]
[[Category: Salvo, M L.di.]]
[[Category: Schirch, V.]]
[[Category: Schirch, V.]]
[[Category: Thiel, D.J.]]
[[Category: Thiel, D J.]]
[[Category: FMN]]
[[Category: FMN]]
[[Category: PO4]]
[[Category: PO4]]
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[[Category: protein-fmn complex]]
[[Category: protein-fmn complex]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:18:29 2008''