1pma

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|SITE=
|SITE=
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|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]
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pma FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pma OCA], [http://www.ebi.ac.uk/pdbsum/1pma PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1pma RCSB]</span>
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[[Category: proteasome]]
[[Category: proteasome]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:26:11 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:01:35 2008''

Revision as of 20:01, 30 March 2008


PDB ID 1pma

Drag the structure with the mouse to rotate
, resolution 3.4Å
Activity: Proteasome endopeptidase complex, with EC number 3.4.25.1
Resources: FirstGlance, OCA, PDBsum, RCSB
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

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