1g77
From Proteopedia
(New page: 200px<br /><applet load="1g77" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g77, resolution 2.10Å" /> '''X-RAY STRUCTURE OF E...) |
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| - | [[Image:1g77.gif|left|200px]]<br /><applet load="1g77" size=" | + | [[Image:1g77.gif|left|200px]]<br /><applet load="1g77" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1g77, resolution 2.10Å" /> | caption="1g77, resolution 2.10Å" /> | ||
'''X-RAY STRUCTURE OF ESCHERICHIA COLI PYRIDOXINE 5`-PHOSPHATE OXIDASE COMPLEXED WITH PYRIDOXAL 5'-PHOSPHATE AT 2.0 A RESOLUTION'''<br /> | '''X-RAY STRUCTURE OF ESCHERICHIA COLI PYRIDOXINE 5`-PHOSPHATE OXIDASE COMPLEXED WITH PYRIDOXAL 5'-PHOSPHATE AT 2.0 A RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Escherichia coli pyridoxine 5'-phosphate oxidase catalyzes the terminal | + | Escherichia coli pyridoxine 5'-phosphate oxidase catalyzes the terminal step in the biosynthesis of pyridoxal 5'-phosphate by the FMN oxidation of pyridoxine 5'-phosphate forming FMNH(2) and H(2)O(2). Recent studies have shown that in addition to the active site, pyridoxine 5'-phosphate oxidase contains a non-catalytic site that binds pyridoxal 5'-phosphate tightly. The crystal structure of pyridoxine 5'-phosphate oxidase from E. coli with one or two molecules of pyridoxal 5'-phosphate bound to each monomer has been determined to 2.0 A resolution. One of the pyridoxal 5'-phosphate molecules is clearly bound at the active site with the aldehyde at C4' of pyridoxal 5'-phosphate near N5 of the bound FMN. A protein conformational change has occurred that partially closes the active site. The orientation of the bound pyridoxal 5'-phosphate suggests that the enzyme catalyzes a hydride ion transfer between C4' of pyridoxal 5'-phosphate and N5 of FMN. When the crystals are soaked with excess pyridoxal 5'-phosphate an additional molecule of this cofactor is also bound about 11 A from the active site. A possible tunnel exists between the two sites so that pyridoxal 5'-phosphate formed at the active site may transfer to the non-catalytic site without passing though the solvent. |
==About this Structure== | ==About this Structure== | ||
| - | 1G77 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, FMN and PLP 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:// | + | 1G77 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>, <scene name='pdbligand=FMN:'>FMN</scene> and <scene name='pdbligand=PLP:'>PLP</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=1G77 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Pyridoxal 5'-phosphate synthase]] | [[Category: Pyridoxal 5'-phosphate synthase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Musayev, F | + | [[Category: Musayev, F N.]] |
| - | [[Category: Safo, M | + | [[Category: Safo, M K.]] |
| - | [[Category: Salvo, M | + | [[Category: Salvo, M L.di.]] |
[[Category: Schirch, V.]] | [[Category: Schirch, V.]] | ||
[[Category: FMN]] | [[Category: FMN]] | ||
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[[Category: pyridoxine 5'-phosphate]] | [[Category: pyridoxine 5'-phosphate]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:46:51 2008'' |
Revision as of 10:46, 21 February 2008
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X-RAY STRUCTURE OF ESCHERICHIA COLI PYRIDOXINE 5`-PHOSPHATE OXIDASE COMPLEXED WITH PYRIDOXAL 5'-PHOSPHATE AT 2.0 A RESOLUTION
Overview
Escherichia coli pyridoxine 5'-phosphate oxidase catalyzes the terminal step in the biosynthesis of pyridoxal 5'-phosphate by the FMN oxidation of pyridoxine 5'-phosphate forming FMNH(2) and H(2)O(2). Recent studies have shown that in addition to the active site, pyridoxine 5'-phosphate oxidase contains a non-catalytic site that binds pyridoxal 5'-phosphate tightly. The crystal structure of pyridoxine 5'-phosphate oxidase from E. coli with one or two molecules of pyridoxal 5'-phosphate bound to each monomer has been determined to 2.0 A resolution. One of the pyridoxal 5'-phosphate molecules is clearly bound at the active site with the aldehyde at C4' of pyridoxal 5'-phosphate near N5 of the bound FMN. A protein conformational change has occurred that partially closes the active site. The orientation of the bound pyridoxal 5'-phosphate suggests that the enzyme catalyzes a hydride ion transfer between C4' of pyridoxal 5'-phosphate and N5 of FMN. When the crystals are soaked with excess pyridoxal 5'-phosphate an additional molecule of this cofactor is also bound about 11 A from the active site. A possible tunnel exists between the two sites so that pyridoxal 5'-phosphate formed at the active site may transfer to the non-catalytic site without passing though the solvent.
About this Structure
1G77 is a Single protein structure of sequence from Escherichia coli with , and as ligands. Active as Pyridoxal 5'-phosphate synthase, with EC number 1.4.3.5 Full crystallographic information is available from OCA.
Reference
X-ray structure of Escherichia coli pyridoxine 5'-phosphate oxidase complexed with pyridoxal 5'-phosphate at 2.0 A resolution., Safo MK, Musayev FN, di Salvo ML, Schirch V, J Mol Biol. 2001 Jul 20;310(4):817-26. PMID:11453690
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