1izy

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|PDB= 1izy |SIZE=350|CAPTION= <scene name='initialview01'>1izy</scene>, resolution 2.80&Aring;
|PDB= 1izy |SIZE=350|CAPTION= <scene name='initialview01'>1izy</scene>, resolution 2.80&Aring;
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|LIGAND= <scene name='pdbligand=X:2&#39;-DEOXY-N7-(8,9-DIHYDRO-9-HYDROXY-10-DEHYDROXY-AFLATOXIN)GUANOSINE+MONOPHOSPHATE'>X</scene>
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|ACTIVITY=
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|RELATEDENTRY=[[1izz|1IZZ]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1izy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1izy OCA], [http://www.ebi.ac.uk/pdbsum/1izy PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1izy RCSB]</span>
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[[Category: alpha-beta sandwitch]]
[[Category: alpha-beta sandwitch]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:57:08 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:26:59 2008''

Revision as of 18:26, 30 March 2008


PDB ID 1izy

Drag the structure with the mouse to rotate
, resolution 2.80Å
Ligands:
Related: 1IZZ


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal structure of Hsp31


Overview

Human DJ-1 and Escherichia coli Hsp31 belong to ThiJ/PfpI family, whose members contain a conserved domain. DJ-1 is associated with autosomal recessive early onset parkinsonism and Hsp31 is a molecular chaperone. Structural comparisons between DJ-1, Hsp31, and an Archaea protease, a member of ThiJ/PfpI family, lead to the identification of the chaperone activity of DJ-1 and the proteolytic activity of Hsp31. Moreover, the comparisons provide insights into how the functional diversity is realized in proteins that share an evolutionarily conserved domain. On the basis of the chaperone activity the possible role of DJ-1 in the pathogenesis of Parkinson's disease is discussed.

About this Structure

1IZY is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Crystal structures of human DJ-1 and Escherichia coli Hsp31, which share an evolutionarily conserved domain., Lee SJ, Kim SJ, Kim IK, Ko J, Jeong CS, Kim GH, Park C, Kang SO, Suh PG, Lee HS, Cha SS, J Biol Chem. 2003 Nov 7;278(45):44552-9. Epub 2003 Aug 25. PMID:12939276

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