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| [[Image:1pma.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1pma| PDB=1pma | SCENE= }} | | {{STRUCTURE_1pma| PDB=1pma | SCENE= }} |
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| '''PROTEASOME FROM THERMOPLASMA ACIDOPHILUM'''
| | ===PROTEASOME FROM THERMOPLASMA ACIDOPHILUM=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_7725097}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 7725097 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_7725097}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Protease]] | | [[Category: Protease]] |
| [[Category: Proteasome]] | | [[Category: Proteasome]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:14:40 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 06:52:06 2008'' |
