2yxt

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(New page: 200px<br /><applet load="2yxt" size="350" color="white" frame="true" align="right" spinBox="true" caption="2yxt, resolution 2.0&Aring;" /> '''Human Pyridoxal Kinas...)
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[[Image:2yxt.jpg|left|200px]]<br /><applet load="2yxt" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2yxt.jpg|left|200px]]
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caption="2yxt, resolution 2.0&Aring;" />
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'''Human Pyridoxal Kinase'''<br />
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{{Structure
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|PDB= 2yxt |SIZE=350|CAPTION= <scene name='initialview01'>2yxt</scene>, resolution 2.0&Aring;
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|SITE= <scene name='pdbsite=AC1:Na+Binding+Site+For+Residue+A+1314'>AC1</scene>, <scene name='pdbsite=AC2:Na+Binding+Site+For+Residue+B+1316'>AC2</scene>, <scene name='pdbsite=AC3:Po4+Binding+Site+For+Residue+A+1319'>AC3</scene>, <scene name='pdbsite=AC4:Po4+Binding+Site+For+Residue+B+1329'>AC4</scene>, <scene name='pdbsite=AC5:Po4+Binding+Site+For+Residue+B+1335'>AC5</scene>, <scene name='pdbsite=AC6:Po4+Binding+Site+For+Residue+B+1337'>AC6</scene>, <scene name='pdbsite=AC7:Po4+Binding+Site+For+Residue+B+1347'>AC7</scene>, <scene name='pdbsite=AC8:Po4+Binding+Site+For+Residue+B+1349'>AC8</scene>, <scene name='pdbsite=AC9:Mpd+Binding+Site+For+Residue+A+1001'>AC9</scene>, <scene name='pdbsite=BC1:Mpd+Binding+Site+For+Residue+A+1003'>BC1</scene>, <scene name='pdbsite=BC2:Mpd+Binding+Site+For+Residue+A+1005'>BC2</scene>, <scene name='pdbsite=BC3:Mpd+Binding+Site+For+Residue+A+1009'>BC3</scene>, <scene name='pdbsite=BC4:Mpd+Binding+Site+For+Residue+A+1013'>BC4</scene>, <scene name='pdbsite=BC5:Mpd+Binding+Site+For+Residue+B+1023'>BC5</scene>, <scene name='pdbsite=BC6:Mpd+Binding+Site+For+Residue+B+1025'>BC6</scene>, <scene name='pdbsite=BC7:Mpd+Binding+Site+For+Residue+B+1027'>BC7</scene>, <scene name='pdbsite=BC8:Mpd+Binding+Site+For+Residue+B+1031'>BC8</scene>, <scene name='pdbsite=BC9:Mpd+Binding+Site+For+Residue+B+1033'>BC9</scene>, <scene name='pdbsite=CC1:Mpd+Binding+Site+For+Residue+B+1039'>CC1</scene>, <scene name='pdbsite=CC2:Mpd+Binding+Site+For+Residue+B+1041'>CC2</scene>, <scene name='pdbsite=CC3:Mpd+Binding+Site+For+Residue+B+1045'>CC3</scene> and <scene name='pdbsite=CC4:Mpd+Binding+Site+For+Residue+B+1053'>CC4</scene>
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|LIGAND= <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> and <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>
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|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]
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|GENE= PDXK, PKH, PNK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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}}
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'''Human Pyridoxal Kinase'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2YXT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NA:'>NA</scene>, <scene name='pdbligand=PO4:'>PO4</scene> and <scene name='pdbligand=MPD:'>MPD</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] Known structural/functional Sites: <scene name='pdbsite=AC1:Na+Binding+Site+For+Residue+A+1314'>AC1</scene>, <scene name='pdbsite=AC2:Na+Binding+Site+For+Residue+B+1316'>AC2</scene>, <scene name='pdbsite=AC3:Po4+Binding+Site+For+Residue+A+1319'>AC3</scene>, <scene name='pdbsite=AC4:Po4+Binding+Site+For+Residue+B+1329'>AC4</scene>, <scene name='pdbsite=AC5:Po4+Binding+Site+For+Residue+B+1335'>AC5</scene>, <scene name='pdbsite=AC6:Po4+Binding+Site+For+Residue+B+1337'>AC6</scene>, <scene name='pdbsite=AC7:Po4+Binding+Site+For+Residue+B+1347'>AC7</scene>, <scene name='pdbsite=AC8:Po4+Binding+Site+For+Residue+B+1349'>AC8</scene>, <scene name='pdbsite=AC9:Mpd+Binding+Site+For+Residue+A+1001'>AC9</scene>, <scene name='pdbsite=BC1:Mpd+Binding+Site+For+Residue+A+1003'>BC1</scene>, <scene name='pdbsite=BC2:Mpd+Binding+Site+For+Residue+A+1005'>BC2</scene>, <scene name='pdbsite=BC3:Mpd+Binding+Site+For+Residue+A+1009'>BC3</scene>, <scene name='pdbsite=BC4:Mpd+Binding+Site+For+Residue+A+1013'>BC4</scene>, <scene name='pdbsite=BC5:Mpd+Binding+Site+For+Residue+B+1023'>BC5</scene>, <scene name='pdbsite=BC6:Mpd+Binding+Site+For+Residue+B+1025'>BC6</scene>, <scene name='pdbsite=BC7:Mpd+Binding+Site+For+Residue+B+1027'>BC7</scene>, <scene name='pdbsite=BC8:Mpd+Binding+Site+For+Residue+B+1031'>BC8</scene>, <scene name='pdbsite=BC9:Mpd+Binding+Site+For+Residue+B+1033'>BC9</scene>, <scene name='pdbsite=CC1:Mpd+Binding+Site+For+Residue+B+1039'>CC1</scene>, <scene name='pdbsite=CC2:Mpd+Binding+Site+For+Residue+B+1041'>CC2</scene>, <scene name='pdbsite=CC3:Mpd+Binding+Site+For+Residue+B+1045'>CC3</scene> and <scene name='pdbsite=CC4:Mpd+Binding+Site+For+Residue+B+1053'>CC4</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YXT OCA].
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2YXT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YXT OCA].
==Reference==
==Reference==
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Crystal Structure of human pyridoxal kinase: structural basis of M(+) and M(2+) activation., Musayev FN, di Salvo ML, Ko TP, Gandhi AK, Goswami A, Schirch V, Safo MK, Protein Sci. 2007 Oct;16(10):2184-94. Epub 2007 Aug 31. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17766369 17766369]
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Crystal Structure of human pyridoxal kinase: structural basis of M(+) and M(2+) activation., Musayev FN, di Salvo ML, Ko TP, Gandhi AK, Goswami A, Schirch V, Safo MK, Protein Sci. 2007 Oct;16(10):2184-94. Epub 2007 Aug 31. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17766369 17766369]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Pyridoxal kinase]]
[[Category: Pyridoxal kinase]]
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[[Category: transferase]]
[[Category: transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Mar 14 09:37:01 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:50:11 2008''

Revision as of 16:50, 20 March 2008

Image:2yxt.jpg


PDB ID 2yxt

Drag the structure with the mouse to rotate
, resolution 2.0Å
Sites: , , , , , , , , , , , , , , , , , , , , and
Ligands: , and
Gene: PDXK, PKH, PNK (Homo sapiens)
Activity: Pyridoxal kinase, with EC number 2.7.1.35
Coordinates: save as pdb, mmCIF, xml



Human Pyridoxal Kinase


Overview

Pyridoxal kinase catalyzes the transfer of a phosphate group from ATP to the 5' alcohol of pyridoxine, pyridoxamine, and pyridoxal. In this work, kinetic studies were conducted to examine monovalent cation dependence of human pyridoxal kinase kinetic parameters. The results show that hPLK affinity for ATP and PL is increased manyfold in the presence of K(+) when compared to Na(+); however, the maximal activity of the Na(+) form of the enzyme is more than double the activity in the presence of K(+). Other monovalent cations, Li(+), Cs(+), and Rb(+) do not show significant activity. We have determined the crystal structure of hPLK in the unliganded form, and in complex with MgATP to 2.0 and 2.2 A resolution, respectively. Overall, the two structures show similar open conformation, and likely represent the catalytically idle state. The crystal structure of the MgATP complex also reveals Mg(2+) and Na(+) acting in tandem to anchor the ATP at the active site. Interestingly, the active site of hPLK acts as a sink to bind several molecules of MPD. The features of monovalent and divalent metal cation binding, active site structure, and vitamin B6 specificity are discussed in terms of the kinetic and structural studies, and are compared with those of the sheep and Escherichia coli enzymes.

About this Structure

2YXT is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal Structure of human pyridoxal kinase: structural basis of M(+) and M(2+) activation., Musayev FN, di Salvo ML, Ko TP, Gandhi AK, Goswami A, Schirch V, Safo MK, Protein Sci. 2007 Oct;16(10):2184-94. Epub 2007 Aug 31. PMID:17766369

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