2ddw: Difference between revisions

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[[Image:2ddw.gif|left|200px]]<br /><applet load="2ddw" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:2ddw.gif|left|200px]]
caption="2ddw, resolution 3.20&Aring;" />
 
'''Crystal Structure of Pyridoxal Kinase from the Escherichia coli PdxK gene complexed with pyridoxal at 3.2 A resolution'''<br />
{{Structure
|PDB= 2ddw |SIZE=350|CAPTION= <scene name='initialview01'>2ddw</scene>, resolution 3.20&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=PXL:3-HYDROXY-5-(HYDROXYMETHYL)-2-METHYLISONICOTINALDEHYDE'>PXL</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]
|GENE= PdxK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
}}
 
'''Crystal Structure of Pyridoxal Kinase from the Escherichia coli PdxK gene complexed with pyridoxal at 3.2 A resolution'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
2DDW 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=PXL:'>PXL</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=2DDW OCA].  
2DDW is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DDW OCA].  


==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16740960 16740960]
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:[http://www.ncbi.nlm.nih.gov/pubmed/16740960 16740960]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Pyridoxal kinase]]
[[Category: Pyridoxal kinase]]
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[[Category: vitamin b6]]
[[Category: vitamin b6]]


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Revision as of 17:26, 20 March 2008

File:2ddw.gif


PDB ID 2ddw

Drag the structure with the mouse to rotate
, resolution 3.20Å
Ligands:
Gene: PdxK (Escherichia coli)
Activity: Pyridoxal kinase, with EC number 2.7.1.35
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of Pyridoxal Kinase from the Escherichia coli PdxK gene complexed with pyridoxal at 3.2 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

2DDW 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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