1ik7

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[[Image:1ik7.jpg|left|200px]]<br /><applet load="1ik7" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ik7.jpg|left|200px]]
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caption="1ik7, resolution 2.30&Aring;" />
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'''Crystal Structure of the Uncomplexed Pelle Death Domain'''<br />
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{{Structure
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|PDB= 1ik7 |SIZE=350|CAPTION= <scene name='initialview01'>1ik7</scene>, resolution 2.30&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene> and <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1]
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|GENE= pelle ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 Drosophila melanogaster])
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}}
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'''Crystal Structure of the Uncomplexed Pelle Death Domain'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1IK7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] with <scene name='pdbligand=TRS:'>TRS</scene> and <scene name='pdbligand=MPD:'>MPD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IK7 OCA].
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1IK7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IK7 OCA].
==Reference==
==Reference==
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Cosolvent-induced transformation of a death domain tertiary structure., Xiao T, Gardner KH, Sprang SR, Proc Natl Acad Sci U S A. 2002 Aug 20;99(17):11151-6. Epub 2002 Aug 12. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12177432 12177432]
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Cosolvent-induced transformation of a death domain tertiary structure., Xiao T, Gardner KH, Sprang SR, Proc Natl Acad Sci U S A. 2002 Aug 20;99(17):11151-6. Epub 2002 Aug 12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12177432 12177432]
[[Category: Drosophila melanogaster]]
[[Category: Drosophila melanogaster]]
[[Category: Non-specific serine/threonine protein kinase]]
[[Category: Non-specific serine/threonine protein kinase]]
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[[Category: structural transition]]
[[Category: structural transition]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:12:46 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:51:26 2008''

Revision as of 09:51, 20 March 2008


PDB ID 1ik7

Drag the structure with the mouse to rotate
, resolution 2.30Å
Ligands: and
Gene: pelle (Drosophila melanogaster)
Activity: Non-specific serine/threonine protein kinase, with EC number 2.7.11.1
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of the Uncomplexed Pelle Death Domain


Overview

The death domain (DD) of the protein kinase Pelle adopts a six-helix bundle fold in the crystal structure of the complex with its dimerization partner, Tube-DD. However, in crystals obtained from a solution of 45% 2-methyl-2,4-pentanediol (MPD), the C-terminal half of Pelle-DD folds into a single helix, and the N-terminal half of the molecule is disordered. The helical segment forms an antiparallel dimer with the corresponding helix of a symmetry-related molecule, and together they form extensive lattice interactions similar in number, composition, and buried surface to those in the six-helix bundle of the native fold. Secondary structure analysis by heteronuclear nuclear magnetic resonance spectroscopy (NMR) demonstrates that Pelle-DD adopts a six-helix bundle fold in aqueous solution. The fold is perturbed by MPD, with the largest chemical shift changes in one helix and two loop regions that encompass the Tube-DD binding site. Pelle-DD is stable to urea denaturation with a folding free energy of 7.9 kcal/mol at 25 degrees C but is destabilized, with loss of urea binding sites, in the presence of MPD. The data are consistent with a cosolvent denaturation model in which MPD denatures the N terminus of Pelle-DD but induces the C terminus to form a more compact structure and aggregate. A similar perturbation in vivo might occur at the plasma membrane and could have consequences for Pelle-mediated regulation. Generally, crystallographers should be aware that high concentrations of MPD or related cosolvents can alter the tertiary structure of susceptible proteins.

About this Structure

1IK7 is a Single protein structure of sequence from Drosophila melanogaster. Full crystallographic information is available from OCA.

Reference

Cosolvent-induced transformation of a death domain tertiary structure., Xiao T, Gardner KH, Sprang SR, Proc Natl Acad Sci U S A. 2002 Aug 20;99(17):11151-6. Epub 2002 Aug 12. PMID:12177432

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