1d7k: Difference between revisions
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'''CRYSTAL STRUCTURE OF HUMAN ORNITHINE DECARBOXYLASE AT 2.1 ANGSTROMS RESOLUTION''' | {{Structure | ||
|PDB= 1d7k |SIZE=350|CAPTION= <scene name='initialview01'>1d7k</scene>, resolution 2.1Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Ornithine_decarboxylase Ornithine decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.17 4.1.1.17] | |||
|GENE= | |||
}} | |||
'''CRYSTAL STRUCTURE OF HUMAN ORNITHINE DECARBOXYLASE AT 2.1 ANGSTROMS RESOLUTION''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1D7K is a [ | 1D7K is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D7K OCA]. | ||
==Reference== | ==Reference== | ||
Crystal structure of human ornithine decarboxylase at 2.1 A resolution: structural insights to antizyme binding., Almrud JJ, Oliveira MA, Kern AD, Grishin NV, Phillips MA, Hackert ML, J Mol Biol. 2000 Jan 7;295(1):7-16. PMID:[http:// | Crystal structure of human ornithine decarboxylase at 2.1 A resolution: structural insights to antizyme binding., Almrud JJ, Oliveira MA, Kern AD, Grishin NV, Phillips MA, Hackert ML, J Mol Biol. 2000 Jan 7;295(1):7-16. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10623504 10623504] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Ornithine decarboxylase]] | [[Category: Ornithine decarboxylase]] | ||
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[[Category: sheet-domain]] | [[Category: sheet-domain]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:34:03 2008'' | ||
Revision as of 11:34, 20 March 2008
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| , resolution 2.1Å | |||||||
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| Activity: | Ornithine decarboxylase, with EC number 4.1.1.17 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF HUMAN ORNITHINE DECARBOXYLASE AT 2.1 ANGSTROMS RESOLUTION
OverviewOverview
The polyamines spermidine and spermine are ubiquitous and required for cell growth and differentiation in eukaryotes. Ornithine decarboxylase (ODC, EC 4.1.1.17) performs the first step in polyamine biosynthesis, the decarboxylation of ornithine to putrescine. Elevated polyamine levels can lead to down-regulation of ODC activity by enhancing the translation of antizyme mRNA, resulting in subsequent binding of antizyme to ODC monomers which targets ODC for proteolysis by the 26S proteasome.The crystal structure of ornithine decarboxylase from human liver has been determined to 2.1 A resolution by molecular replacement using truncated mouse ODC (Delta425-461) as the search model and refined to a crystallographic R-factor of 21.2% and an R-free value of 28.8%. The human ODC model includes several regions that are disordered in the mouse ODC crystal structure, including one of two C-terminal basal degradation elements that have been demonstrated to independently collaborate with antizyme binding to target ODC for degradation by the 26S proteasome.The crystal structure of human ODC suggests that the C terminus, which contains basal degradation elements necessary for antizyme-induced proteolysis, is not buried by the structural core of homodimeric ODC as previously proposed. Analysis of the solvent-accessible surface area, surface electrostatic potential, and the conservation of primary sequence between human ODC and Trypanosoma brucei ODC provides clues to the identity of potential protein-binding-determinants in the putative antizyme binding element in human ODC.
DiseaseDisease
Known disease associated with this structure: Colonic adenoma recurrence, reduced risk of OMIM:[165640]
About this StructureAbout this Structure
1D7K is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of human ornithine decarboxylase at 2.1 A resolution: structural insights to antizyme binding., Almrud JJ, Oliveira MA, Kern AD, Grishin NV, Phillips MA, Hackert ML, J Mol Biol. 2000 Jan 7;295(1):7-16. PMID:10623504
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