1nw1: Difference between revisions

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New page: left|200px<br /><applet load="1nw1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nw1, resolution 2.02Å" /> '''Crystal Structure of...
 
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[[Image:1nw1.jpg|left|200px]]<br /><applet load="1nw1" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1nw1.jpg|left|200px]]<br /><applet load="1nw1" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1nw1, resolution 2.02&Aring;" />
caption="1nw1, resolution 2.02&Aring;" />
'''Crystal Structure of Choline Kinase'''<br />
'''Crystal Structure of Choline Kinase'''<br />


==Overview==
==Overview==
Choline kinase catalyzes the ATP-dependent phosphorylation of choline, the, first committed step in the CDP-choline pathway for the biosynthesis of, phosphatidylcholine. The 2.0 A crystal structure of a choline kinase from, C. elegans (CKA-2) reveals that the enzyme is a homodimeric protein with, each monomer organized into a two-domain fold. The structure is remarkably, similar to those of protein kinases and aminoglycoside, phosphotransferases, despite no significant similarity in amino acid, sequence. Comparisons to the structures of other kinases suggest that ATP, binds to CKA-2 in a pocket formed by highly conserved and catalytically, important residues. In addition, a choline binding site is proposed to be, near the ATP binding pocket and formed by several structurally flexible, loops.
Choline kinase catalyzes the ATP-dependent phosphorylation of choline, the first committed step in the CDP-choline pathway for the biosynthesis of phosphatidylcholine. The 2.0 A crystal structure of a choline kinase from C. elegans (CKA-2) reveals that the enzyme is a homodimeric protein with each monomer organized into a two-domain fold. The structure is remarkably similar to those of protein kinases and aminoglycoside phosphotransferases, despite no significant similarity in amino acid sequence. Comparisons to the structures of other kinases suggest that ATP binds to CKA-2 in a pocket formed by highly conserved and catalytically important residues. In addition, a choline binding site is proposed to be near the ATP binding pocket and formed by several structurally flexible loops.


==About this Structure==
==About this Structure==
1NW1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Choline_kinase Choline kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.32 2.7.1.32] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NW1 OCA].  
1NW1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Choline_kinase Choline kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.32 2.7.1.32] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NW1 OCA].  


==Reference==
==Reference==
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[[Category: protein kinase fold]]
[[Category: protein kinase fold]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:10:40 2008''

Revision as of 15:10, 21 February 2008

File:1nw1.jpg


1nw1, resolution 2.02Å

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Crystal Structure of Choline Kinase

OverviewOverview

Choline kinase catalyzes the ATP-dependent phosphorylation of choline, the first committed step in the CDP-choline pathway for the biosynthesis of phosphatidylcholine. The 2.0 A crystal structure of a choline kinase from C. elegans (CKA-2) reveals that the enzyme is a homodimeric protein with each monomer organized into a two-domain fold. The structure is remarkably similar to those of protein kinases and aminoglycoside phosphotransferases, despite no significant similarity in amino acid sequence. Comparisons to the structures of other kinases suggest that ATP binds to CKA-2 in a pocket formed by highly conserved and catalytically important residues. In addition, a choline binding site is proposed to be near the ATP binding pocket and formed by several structurally flexible loops.

About this StructureAbout this Structure

1NW1 is a Single protein structure of sequence from Caenorhabditis elegans with as ligand. Active as Choline kinase, with EC number 2.7.1.32 Full crystallographic information is available from OCA.

ReferenceReference

The crystal structure of choline kinase reveals a eukaryotic protein kinase fold., Peisach D, Gee P, Kent C, Xu Z, Structure. 2003 Jun;11(6):703-13. PMID:12791258

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