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1pma
From Proteopedia
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| - | [[Image:1pma.gif|left|200px]] | + | [[Image:1pma.gif|left|200px]] |
| - | + | ||
| - | '''PROTEASOME FROM THERMOPLASMA ACIDOPHILUM''' | + | {{Structure |
| + | |PDB= 1pma |SIZE=350|CAPTION= <scene name='initialview01'>1pma</scene>, resolution 3.4Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Proteasome_endopeptidase_complex Proteasome endopeptidase complex], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.25.1 3.4.25.1] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''PROTEASOME FROM THERMOPLASMA ACIDOPHILUM''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1PMA is a [ | + | 1PMA is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PMA OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution., Lowe J, Stock D, Jap B, Zwickl P, Baumeister W, Huber R, Science. 1995 Apr 28;268(5210):533-9. PMID:[http:// | + | Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution., Lowe J, Stock D, Jap B, Zwickl P, Baumeister W, Huber R, Science. 1995 Apr 28;268(5210):533-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7725097 7725097] |
[[Category: Proteasome endopeptidase complex]] | [[Category: Proteasome endopeptidase complex]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: proteasome]] | [[Category: proteasome]] | ||
| - | ''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 13:26:11 2008'' |
Revision as of 11:26, 20 March 2008
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| , resolution 3.4Å | |||||||
|---|---|---|---|---|---|---|---|
| Activity: | Proteasome endopeptidase complex, with EC number 3.4.25.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
PROTEASOME FROM THERMOPLASMA ACIDOPHILUM
Overview
The three-dimensional structure of the proteasome from the archaebacterium Thermoplasma acidophilum has been elucidated by x-ray crystallographic analysis by means of isomorphous replacement and cyclic averaging. The atomic model was built and refined to a crystallographic R factor of 22.1 percent. The 673-kilodalton protease complex consists of 14 copies of two different subunits, alpha and beta, forming a barrel-shaped structure of four stacked rings. The two inner rings consist of seven beta subunits each, and the two outer rings consist of seven alpha subunits each. A narrow channel controls access to the three inner compartments. The alpha 7 beta 7 beta 7 alpha 7 subunit assembly has 72-point group symmetry. The structures of the alpha and beta subunits are similar, consisting of a core of two antiparallel beta sheets that is flanked by alpha helices on both sides. The binding of a peptide aldehyde inhibitor marks the active site in the central cavity at the amino termini of the beta subunits and suggests a novel proteolytic mechanism.
About this Structure
1PMA is a Protein complex structure of sequences from Thermoplasma acidophilum. Full crystallographic information is available from OCA.
Reference
Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution., Lowe J, Stock D, Jap B, Zwickl P, Baumeister W, Huber R, Science. 1995 Apr 28;268(5210):533-9. PMID:7725097
Page seeded by OCA on Thu Mar 20 13:26:11 2008
