2ddm: Difference between revisions
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|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene> | |LIGAND= <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene> | ||
|ACTIVITY= [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] | |ACTIVITY= <span class='plainlinks'>[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] </span> | ||
|GENE= pdxK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= pdxK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[2ddo|2DDO]], [[2ddw|2DDW]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ddm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ddm OCA], [http://www.ebi.ac.uk/pdbsum/2ddm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ddm RCSB]</span> | |||
}} | }} | ||
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[[Category: Salvo, M L.di.]] | [[Category: Salvo, M L.di.]] | ||
[[Category: Schirch, V.]] | [[Category: Schirch, V.]] | ||
[[Category: phosphorylation]] | [[Category: phosphorylation]] | ||
[[Category: pyridoxal 5'-phosphate]] | [[Category: pyridoxal 5'-phosphate]] | ||
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[[Category: vitamin b6]] | [[Category: vitamin b6]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:33:18 2008'' | ||
Revision as of 02:33, 31 March 2008
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| , resolution 2.10Å | |||||||
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| Ligands: | |||||||
| Gene: | pdxK (Escherichia coli) | ||||||
| Activity: | Pyridoxal kinase, with EC number 2.7.1.35 | ||||||
| Related: | 2DDO, 2DDW
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of Pyridoxal Kinase from the Escherichia coli PdxK gene at 2.1 A resolution
OverviewOverview
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 StructureAbout this Structure
2DDM is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
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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