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PDBsum entry 1pma
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Contents |
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(+ 8 more)
221 a.a.
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(+ 8 more)
203 a.a.
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Crystal structure of the 20s proteasome from the archaeon t. Acidophilum at 3.4 a resolution.
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Authors
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J.Löwe,
D.Stock,
B.Jap,
P.Zwickl,
W.Baumeister,
R.Huber.
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Ref.
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Science, 1995,
268,
533-539.
[DOI no: ]
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PubMed id
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Abstract
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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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Secondary reference #1
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Title
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Crystal structure of p22 tailspike protein: interdigitated subunits in a thermostable trimer.
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Authors
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S.Steinbacher,
R.Seckler,
S.Miller,
B.Steipe,
R.Huber,
P.Reinemer.
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Ref.
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Science, 1994,
265,
383-386.
[DOI no: ]
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PubMed id
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