1g79: Difference between revisions

Revision as of 13:46, 21 February 2008

X-RAY STRUCTURE OF ESCHERICHIA COLI PYRIDOXINE 5'-PHOSPHATE OXIDASE COMPLEXED WITH PYRIDOXAL 5'-PHOSPHATE AT 2.0 A RESOLUTION

OverviewOverview

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 StructureAbout this Structure

1G79 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.

ReferenceReference

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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-[[Image:1g79.gif|left|200px]]<br /><applet load="1g79" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1g79.gif|left|200px]]<br /><applet load="1g79" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1g79, resolution 2.00&Aring;" />
 '''X-RAY STRUCTURE OF ESCHERICHIA COLI PYRIDOXINE 5'-PHOSPHATE OXIDASE COMPLEXED WITH PYRIDOXAL 5'-PHOSPHATE AT 2.0 A RESOLUTION'''<br />
 ==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.
+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==
-G79 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, PLP and BME 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=1G79 OCA].
+G79 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>, <scene name='pdbligand=PLP:'>PLP</scene> and <scene name='pdbligand=BME:'>BME</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=1G79 OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Pyridoxal 5'-phosphate synthase]]
 [[Category: Single protein]]
-[[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: BME]]
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 [[Category: pyridoxine 5'-phosphate]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:46:40 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:46:51 2008''