1jyl

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[[Image:1jyl.gif|left|200px]]
[[Image:1jyl.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1jyl |SIZE=350|CAPTION= <scene name='initialview01'>1jyl</scene>, resolution 2.4&Aring;
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The line below this paragraph, containing "STRUCTURE_1jyl", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=CDC:[2-CYTIDYLATE-O&#39;-PHOSPHONYLOXYL]-ETHYL-TRIMETHYL-AMMONIUM'>CDC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY=
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or leave the SCENE parameter empty for the default display.
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|GENE= LicC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1313 Streptococcus pneumoniae])
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-->
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|DOMAIN=
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{{STRUCTURE_1jyl| PDB=1jyl | SCENE= }}
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|RELATEDENTRY=[[1jyk|1JYK]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jyl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jyl OCA], [http://www.ebi.ac.uk/pdbsum/1jyl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jyl RCSB]</span>
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}}
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'''Catalytic Mechanism of CTP:phosphocholine Cytidylytransferase from Streptococcus pneumoniae (LicC)'''
'''Catalytic Mechanism of CTP:phosphocholine Cytidylytransferase from Streptococcus pneumoniae (LicC)'''
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[[Category: Yun, M.]]
[[Category: Yun, M.]]
[[Category: 3d structure]]
[[Category: 3d structure]]
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[[Category: ctp:phosphocholine cytidylyltransferase]]
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[[Category: Ctp:phosphocholine cytidylyltransferase]]
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[[Category: licc]]
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[[Category: Licc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:04:55 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:40:48 2008''
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Revision as of 19:04, 2 May 2008

Image:1jyl.gif

Template:STRUCTURE 1jyl

Catalytic Mechanism of CTP:phosphocholine Cytidylytransferase from Streptococcus pneumoniae (LicC)


Overview

Pneumococcal LicC is a member of the nucleoside triphosphate transferase superfamily and catalyzes the transfer of a cytidine monophosphate from CTP to phosphocholine to form CDP-choline. The structures of apo-LicC and the LicC-CDP-choline-Mg(2+) ternary complex were determined, and the comparison of these structures reveals a significant conformational change driven by the multivalent coordination of Mg(2+). The key event is breaking the Glu(216)-Arg(129) salt bridge, which triggers the coalescence of four individual beta-strands into two extended beta-sheets. These movements reorient the side chains of Trp(136) and Tyr(190) for the optimal binding and alignment of the phosphocholine moiety. Consistent with these conformational changes, LicC operates via a compulsory ordered kinetic mechanism. The structures explain the substrate specificity of LicC for CTP and phosphocholine and implicate a direct role for Mg(2+) in aligning phosphocholine for in-line nucleophilic attack and stabilizing the negative charge that develops in the pentacoordinate transition state. These results provide a structural basis for assigning a specific role for magnesium in the catalytic mechanism of pneumococcal LicC.

About this Structure

1JYL is a Single protein structure of sequence from Streptococcus pneumoniae. Full crystallographic information is available from OCA.

Reference

Structure and mechanism of CTP:phosphocholine cytidylyltransferase (LicC) from Streptococcus pneumoniae., Kwak BY, Zhang YM, Yun M, Heath RJ, Rock CO, Jackowski S, Park HW, J Biol Chem. 2002 Feb 8;277(6):4343-50. Epub 2001 Nov 12. PMID:11706035 Page seeded by OCA on Fri May 2 22:04:55 2008

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