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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'''Crystal Structure of Choline Kinase'''<br />


==Overview==
==Crystal Structure of Choline Kinase==
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.
<StructureSection load='1nw1' size='340' side='right'caption='[[1nw1]], [[Resolution|resolution]] 2.02&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1nw1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NW1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NW1 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.02&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1nw1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nw1 OCA], [https://pdbe.org/1nw1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nw1 RCSB], [https://www.ebi.ac.uk/pdbsum/1nw1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nw1 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CKA2_CAEEL CKA2_CAEEL] Catalyzes the first step in phosphatidylcholine biosynthesis. May contribute to phosphatidylethanolamine biosynthesis. Phosphorylates choline and ethanolamine but the activity is much higher with choline.<ref>PMID:12758145</ref> <ref>PMID:14960577</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nw/1nw1_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1nw1 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
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].
*[[Choline kinase 3D structures|Choline kinase 3D structures]]
 
*[[Hemoglobin 3D structures|Hemoglobin 3D structures]]
==Reference==
== References ==
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12791258 12791258]
<references/>
__TOC__
</StructureSection>
[[Category: Caenorhabditis elegans]]
[[Category: Caenorhabditis elegans]]
[[Category: Choline kinase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Gee P]]
[[Category: Gee, P.]]
[[Category: Kent C]]
[[Category: Kent, C.]]
[[Category: Peisach D]]
[[Category: Peisach, D.]]
[[Category: Xu Z]]
[[Category: Xu, Z.]]
[[Category: CA]]
[[Category: choline kinase]]
[[Category: phospholipid synthesis]]
[[Category: protein kinase fold]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 23:54:19 2007''

Latest revision as of 10:59, 14 February 2024

Crystal Structure of Choline KinaseCrystal Structure of Choline Kinase

Structural highlights

1nw1 is a 2 chain structure with sequence from Caenorhabditis elegans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.02Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CKA2_CAEEL Catalyzes the first step in phosphatidylcholine biosynthesis. May contribute to phosphatidylethanolamine biosynthesis. Phosphorylates choline and ethanolamine but the activity is much higher with choline.[1] [2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Gee P, Kent C. Multiple isoforms of choline kinase from Caenorhabditis elegans: cloning, expression, purification, and characterization. Biochim Biophys Acta. 2003 May 30;1648(1-2):33-42. PMID:12758145 doi:10.1016/s1570-9639(03)00106-7
  2. ↑ Yuan C, Kent C. Identification of critical residues of choline kinase A2 from Caenorhabditis elegans. J Biol Chem. 2004 Apr 23;279(17):17801-9. PMID:14960577 doi:10.1074/jbc.M401382200

1nw1, resolution 2.02Å

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