1td2
From Proteopedia
(New page: 200px<br /><applet load="1td2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1td2, resolution 2.22Å" /> '''Crystal Structure of...) |
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| - | [[Image:1td2.jpg|left|200px]]<br /><applet load="1td2" size=" | + | [[Image:1td2.jpg|left|200px]]<br /><applet load="1td2" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1td2, resolution 2.22Å" /> | caption="1td2, resolution 2.22Å" /> | ||
'''Crystal Structure of the PdxY Protein from Escherichia coli'''<br /> | '''Crystal Structure of the PdxY Protein from Escherichia coli'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of Escherichia coli PdxY, the protein product of the | + | The crystal structure of Escherichia coli PdxY, the protein product of the pdxY gene, has been determined to a 2.2-A resolution. PdxY is a member of the ribokinase superfamily of enzymes and has sequence homology with pyridoxal kinases that phosphorylate pyridoxal at the C-5' hydroxyl. The protein is a homodimer with an active site on each monomer composed of residues that come exclusively from each respective subunit. The active site is filled with a density that fits that of pyridoxal. In monomer A, the ligand appears to be covalently attached to Cys122 as a thiohemiacetal, while in monomer B it is not covalently attached but appears to be partially present as pyridoxal 5'-phosphate. The presence of pyridoxal phosphate and pyridoxal as ligands was confirmed by the activation of aposerine hydroxymethyltransferase after release of the ligand by the denaturation of PdxY. The ligand, which appears to be covalently attached to Cys122, does not dissociate after denaturation of the protein. A detailed comparison (of functional properties, sequence homology, active site and ATP-binding-site residues, and active site flap types) of PdxY with other pyridoxal kinases as well as the ribokinase superfamily in general suggested that PdxY is a member of a new subclass of the ribokinase superfamily. The structure of PdxY also permitted an interpretation of work that was previously published about this enzyme. |
==About this Structure== | ==About this Structure== | ||
| - | 1TD2 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 SO4 and PXL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Pyridoxal_kinase Pyridoxal kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.35 2.7.1.35] Full crystallographic information is available from [http:// | + | 1TD2 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=SO4:'>SO4</scene> and <scene name='pdbligand=PXL:'>PXL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Pyridoxal_kinase Pyridoxal kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.35 2.7.1.35] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TD2 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Hunt, S.]] | [[Category: Hunt, S.]] | ||
| - | [[Category: Musayev, F | + | [[Category: Musayev, F N.]] |
| - | [[Category: Safo, M | + | [[Category: Safo, M K.]] |
| - | [[Category: Salvo, M | + | [[Category: Salvo, M di.]] |
[[Category: Scarsdale, N.]] | [[Category: Scarsdale, N.]] | ||
[[Category: Schirch, V.]] | [[Category: Schirch, V.]] | ||
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[[Category: ribokinase family]] | [[Category: ribokinase family]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:12:15 2008'' |
Revision as of 13:12, 21 February 2008
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Crystal Structure of the PdxY Protein from Escherichia coli
Overview
The crystal structure of Escherichia coli PdxY, the protein product of the pdxY gene, has been determined to a 2.2-A resolution. PdxY is a member of the ribokinase superfamily of enzymes and has sequence homology with pyridoxal kinases that phosphorylate pyridoxal at the C-5' hydroxyl. The protein is a homodimer with an active site on each monomer composed of residues that come exclusively from each respective subunit. The active site is filled with a density that fits that of pyridoxal. In monomer A, the ligand appears to be covalently attached to Cys122 as a thiohemiacetal, while in monomer B it is not covalently attached but appears to be partially present as pyridoxal 5'-phosphate. The presence of pyridoxal phosphate and pyridoxal as ligands was confirmed by the activation of aposerine hydroxymethyltransferase after release of the ligand by the denaturation of PdxY. The ligand, which appears to be covalently attached to Cys122, does not dissociate after denaturation of the protein. A detailed comparison (of functional properties, sequence homology, active site and ATP-binding-site residues, and active site flap types) of PdxY with other pyridoxal kinases as well as the ribokinase superfamily in general suggested that PdxY is a member of a new subclass of the ribokinase superfamily. The structure of PdxY also permitted an interpretation of work that was previously published about this enzyme.
About this Structure
1TD2 is a Single protein structure of sequence from Escherichia coli with and as ligands. Active as Pyridoxal kinase, with EC number 2.7.1.35 Full crystallographic information is available from OCA.
Reference
Crystal structure of the PdxY Protein from Escherichia coli., Safo MK, Musayev FN, Hunt S, di Salvo ML, Scarsdale N, Schirch V, J Bacteriol. 2004 Dec;186(23):8074-82. PMID:15547280
Page seeded by OCA on Thu Feb 21 15:12:15 2008
Categories: Escherichia coli | Pyridoxal kinase | Single protein | Hunt, S. | Musayev, F N. | Safo, M K. | Salvo, M di. | Scarsdale, N. | Schirch, V. | PXL | SO4 | Kinase | Pdxy | Phosphorylation | Ribokinase family
