2ddm
From Proteopedia
(New page: 200px<br /><applet load="2ddm" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ddm, resolution 2.10Å" /> '''Crystal Structure of...) |
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| - | [[Image:2ddm.gif|left|200px]]<br /><applet load="2ddm" size=" | + | [[Image:2ddm.gif|left|200px]]<br /><applet load="2ddm" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2ddm, resolution 2.10Å" /> | caption="2ddm, resolution 2.10Å" /> | ||
'''Crystal Structure of Pyridoxal Kinase from the Escherichia coli PdxK gene at 2.1 A resolution'''<br /> | '''Crystal Structure of Pyridoxal Kinase from the Escherichia coli PdxK gene at 2.1 A resolution'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The pdxK and pdxY genes have been found to code for pyridoxal kinases, enzymes involved in the pyridoxal phosphate salvage pathway. Two pyridoxal | + | The pdxK and pdxY genes have been found to code for pyridoxal kinases, enzymes involved in the pyridoxal phosphate salvage pathway. Two pyridoxal kinase structures have recently been published, including Escherichia coli pyridoxal kinase 2 (ePL kinase 2) and sheep pyridoxal kinase, products of the pdxY and pdxK genes, respectively. We now report the crystal structure of E. coli pyridoxal kinase 1 (ePL kinase 1), encoded by a pdxK gene, and an isoform of ePL kinase 2. The structures were determined in the unliganded and binary complexes with either MgATP or pyridoxal to 2.1-, 2.6-, and 3.2-A resolutions, respectively. The active site of ePL kinase 1 does not show significant conformational change upon binding of either pyridoxal or MgATP. Like sheep PL kinase, ePL kinase 1 exhibits a sequential random mechanism. Unlike sheep pyridoxal kinase, ePL kinase 1 may not tolerate wide variation in the size and chemical nature of the 4' substituent on the substrate. This is the result of differences in a key residue at position 59 on a loop (loop II) that partially forms the active site. Residue 59, which is His in ePL kinase 1, interacts with the formyl group at C-4' of pyridoxal and may also determine if residues from another loop (loop I) can fill the active site in the absence of the substrate. Both loop I and loop II are suggested to play significant roles in the functions of PL kinases. |
==About this Structure== | ==About this Structure== | ||
| - | 2DDM 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 TRS as [http://en.wikipedia.org/wiki/ligand ligand]. 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:// | + | 2DDM 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=TRS:'>TRS</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=2DDM OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Pyridoxal kinase]] | [[Category: Pyridoxal kinase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Claude, J | + | [[Category: Claude, J B.]] |
[[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 L.di.]] |
[[Category: Schirch, V.]] | [[Category: Schirch, V.]] | ||
[[Category: TRS]] | [[Category: TRS]] | ||
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[[Category: vitamin b6]] | [[Category: vitamin b6]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:57:44 2008'' |
Revision as of 14:57, 21 February 2008
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Crystal Structure of Pyridoxal Kinase from the Escherichia coli PdxK gene at 2.1 A resolution
Overview
The pdxK and pdxY genes have been found to code for pyridoxal kinases, enzymes involved in the pyridoxal phosphate salvage pathway. Two pyridoxal kinase structures have recently been published, including Escherichia coli pyridoxal kinase 2 (ePL kinase 2) and sheep pyridoxal kinase, products of the pdxY and pdxK genes, respectively. We now report the crystal structure of E. coli pyridoxal kinase 1 (ePL kinase 1), encoded by a pdxK gene, and an isoform of ePL kinase 2. The structures were determined in the unliganded and binary complexes with either MgATP or pyridoxal to 2.1-, 2.6-, and 3.2-A resolutions, respectively. The active site of ePL kinase 1 does not show significant conformational change upon binding of either pyridoxal or MgATP. Like sheep PL kinase, ePL kinase 1 exhibits a sequential random mechanism. Unlike sheep pyridoxal kinase, ePL kinase 1 may not tolerate wide variation in the size and chemical nature of the 4' substituent on the substrate. This is the result of differences in a key residue at position 59 on a loop (loop II) that partially forms the active site. Residue 59, which is His in ePL kinase 1, interacts with the formyl group at C-4' of pyridoxal and may also determine if residues from another loop (loop I) can fill the active site in the absence of the substrate. Both loop I and loop II are suggested to play significant roles in the functions of PL kinases.
About this Structure
2DDM is a Single protein structure of sequence from Escherichia coli with as ligand. Active as Pyridoxal kinase, with EC number 2.7.1.35 Full crystallographic information is available from OCA.
Reference
Crystal structure of pyridoxal kinase from the Escherichia coli pdxK gene: implications for the classification of pyridoxal kinases., Safo MK, Musayev FN, di Salvo ML, Hunt S, Claude JB, Schirch V, J Bacteriol. 2006 Jun;188(12):4542-52. PMID:16740960
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