1nw1: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
No edit summary
No edit summary
 
Line 3: Line 3:
<StructureSection load='1nw1' size='340' side='right'caption='[[1nw1]], [[Resolution|resolution]] 2.02&Aring;' scene=''>
<StructureSection load='1nw1' size='340' side='right'caption='[[1nw1]], [[Resolution|resolution]] 2.02&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1nw1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Caeel Caeel]. 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>
<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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
</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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Choline_kinase Choline kinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.32 2.7.1.32] </span></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>
<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>
</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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 18: Line 20:
</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].
</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>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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<ref>PMID:12791258</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1nw1" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
Line 35: Line 28:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Caeel]]
[[Category: Caenorhabditis elegans]]
[[Category: Choline kinase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[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: Phospholipid synthesis]]
[[Category: Protein kinase fold]]
[[Category: Transferase]]

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

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=1nw1&oldid=4052704"