1pma

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[[Image:1pma.gif|left|200px]]
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{{STRUCTURE_1pma| PDB=1pma | SCENE= }}
{{STRUCTURE_1pma| PDB=1pma | SCENE= }}
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'''PROTEASOME FROM THERMOPLASMA ACIDOPHILUM'''
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===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.
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(as it appears on PubMed at http://www.pubmed.gov), where 7725097 is the PubMed ID number.
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{{ABSTRACT_PUBMED_7725097}}
==About this Structure==
==About this Structure==
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[[Category: Protease]]
[[Category: Protease]]
[[Category: Proteasome]]
[[Category: Proteasome]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 06:52:06 2008''

Revision as of 03:52, 28 July 2008

Template:STRUCTURE 1pma

PROTEASOME FROM THERMOPLASMA ACIDOPHILUM

Template:ABSTRACT PUBMED 7725097

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

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