1dnl

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|PDB= 1dnl |SIZE=350|CAPTION= <scene name='initialview01'>1dnl</scene>, resolution 1.8&Aring;
|PDB= 1dnl |SIZE=350|CAPTION= <scene name='initialview01'>1dnl</scene>, resolution 1.8&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> and <scene name='pdbligand=FMN:FLAVIN MONONUCLEOTIDE'>FMN</scene>
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|LIGAND= <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>
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|ACTIVITY= [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]
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|ACTIVITY= <span class='plainlinks'>[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] </span>
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dnl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dnl OCA], [http://www.ebi.ac.uk/pdbsum/1dnl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dnl RCSB]</span>
}}
}}
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[[Category: Schirch, V.]]
[[Category: Schirch, V.]]
[[Category: Thiel, D J.]]
[[Category: Thiel, D J.]]
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[[Category: FMN]]
 
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[[Category: PO4]]
 
[[Category: beta barrel]]
[[Category: beta barrel]]
[[Category: oxidoreductase]]
[[Category: oxidoreductase]]
[[Category: protein-fmn complex]]
[[Category: protein-fmn complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:41:20 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:45:01 2008''

Revision as of 16:45, 30 March 2008


PDB ID 1dnl

Drag the structure with the mouse to rotate
, resolution 1.8Å
Ligands: , ,
Activity: Pyridoxal 5'-phosphate synthase, with EC number 1.4.3.5
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



X-RAY STRUCTURE OF ESCHERICHIA COLI PYRIDOXINE 5'-PHOSPHATE OXIDASE COMPLEXED WITH FMN AT 1.8 ANGSTROM RESOLUTION


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.

About this Structure

1DNL is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

X-ray structure of Escherichia coli pyridoxine 5'-phosphate oxidase complexed with FMN at 1.8 A resolution., Safo MK, Mathews I, Musayev FN, di Salvo ML, Thiel DJ, Abraham DJ, Schirch V, Structure. 2000 Jul 15;8(7):751-62. PMID:10903950

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