1jkn: Difference between revisions

Revision as of 21:20, 2 May 2008

Solution Structure of the Nudix Enzyme Diadenosine Tetraphosphate Hydrolase from Lupinus angustifolius Complexed with ATP

OverviewOverview

Ap(4)A hydrolases are Nudix enzymes that regulate intracellular dinucleoside polyphosphate concentrations, implicating them in a range of biological events, including heat shock and metabolic stress. We have demonstrated that ATP x MgF(x) can be used to mimic substrates in the binding site of Ap(4)A hydrolase from Lupinus angustifolius and that, unlike previous substrate analogs, it is in slow exchange with the enzyme. The three-dimensional structure of the enzyme complexed with ATP x MgF(x) was solved and shows significant conformational changes. The substrate binding site of L. angustifolius Ap(4)A hydrolase differs markedly from the two previously published Nudix enzymes, ADP-ribose pyrophosphatase and MutT, despite their common fold and the conservation of active site residues. The majority of residues involved in substrate binding are conserved in asymmetrical Ap(4)A hydrolases from pathogenic bacteria, but are absent in their human counterparts, suggesting that it might be possible to generate compounds that target bacterial, but not human, Ap(4)A hydrolases.

About this StructureAbout this Structure

1JKN is a Single protein structure of sequence from Lupinus angustifolius. Full crystallographic information is available from OCA.

ReferenceReference

The structure of Ap(4)A hydrolase complexed with ATP-MgF(x) reveals the basis of substrate binding., Fletcher JI, Swarbrick JD, Maksel D, Gayler KR, Gooley PR, Structure. 2002 Feb;10(2):205-13. PMID:11839306 Page seeded by OCA on Fri May 2 21:20:20 2008

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OCA

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 [[Image:1jkn.jpg|left|200px]]
- {{Structure
+<!--
-|PDB= 1jkn |SIZE=350|CAPTION= <scene name='initialview01'>1jkn</scene>
+The line below this paragraph, containing "STRUCTURE_1jkn", creates the "Structure Box" on the page.
-|SITE=
+You may change the PDB parameter (which sets the PDB file loaded into the applet)
-|LIGAND= <scene name='pdbligand=ATP:ADENOSINE-5&#39;-TRIPHOSPHATE'>ATP</scene>
+or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Bis(5'-nucleosyl)-tetraphosphatase_(asymmetrical) Bis(5'-nucleosyl)-tetraphosphatase (asymmetrical)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.17 3.6.1.17] </span>
+or leave the SCENE parameter empty for the default display.
-|GENE=
+-->
-|DOMAIN=
+{{STRUCTURE_1jkn|  PDB=1jkn  |  SCENE=  }}
-|RELATEDENTRY=[[1f3y|1F3Y]]
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jkn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jkn OCA], [http://www.ebi.ac.uk/pdbsum/1jkn PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jkn RCSB]</span>
-}}
 '''Solution Structure of the Nudix Enzyme Diadenosine Tetraphosphate Hydrolase from Lupinus angustifolius Complexed with ATP'''
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 ==Reference==
 The structure of Ap(4)A hydrolase complexed with ATP-MgF(x) reveals the basis of substrate binding., Fletcher JI, Swarbrick JD, Maksel D, Gayler KR, Gooley PR, Structure. 2002 Feb;10(2):205-13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11839306 11839306]
-[[Category: Bis(5'-nucleosyl)-tetraphosphatase (asymmetrical)]]
 [[Category: Lupinus angustifolius]]
 [[Category: Single protein]]
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 [[Category: Maksel, D.]]
 [[Category: Swarbrick, J D.]]
-[[Category: alpha-beta-alpha sandwich]]
+[[Category: Alpha-beta-alpha sandwich]]
-[[Category: enzyme-substrate complex]]
+[[Category: Enzyme-substrate complex]]
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 21:20:20 2008''
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:35:04 2008''