2wg5

PROTEASOME-ACTIVATING NUCLEOTIDASE (PAN) N-DOMAIN (57-134) FROM ARCHAEOGLOBUS FULGIDUS FUSED TO GCN4

spinqualitylabelsall models 2wg5, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2wg5 is a 12 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1rb5, 1unt, 1gcm, 1llm, 2zta, 1unw, 1uo2, 1ce9, 2ccf, 1tmz, 1zil, 2ccn, 1w5l, 1rb6, 1unz, 1zij, 1w5k, 1piq, 1unx, 1uny, 1zik, 1ysa, 1w5h, 1ij2, 1unv, 1uo3, 1ij0, 2cce, 1unu, 1w5g, 1ld4, 2b22, 2b1f, 1uo0, 1uo1, 1swi, 1w5i, 2dgc, 2d3e, 1nkn, 1kql, 1gcl, 1zii, 1rb4, 1uo5, 1ihq, 1ij3, 1zta, 1uo4, 1w5j, 1ij1, 1dgc, 1rb1, 1zim, 2bni, 1gzl, 2wg6 Activity: Proteasome ATPase, with EC number 3.6.4.8 Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The proteasome forms the core of the protein quality control system in archaea and eukaryotes and also occurs in one bacterial lineage, the Actinobacteria. Access to its proteolytic compartment is controlled by AAA ATPases, whose N-terminal domains (N domains) are thought to mediate substrate recognition. The N domains of an archaeal proteasomal ATPase, Archaeoglobus fulgidus PAN, and of its actinobacterial homolog, Rhodococcus erythropolis ARC, form hexameric rings, whose subunits consist of an N-terminal coiled coil and a C-terminal OB domain. In ARC-N, the OB domains are duplicated and form separate rings. PAN-N and ARC-N can act as chaperones, preventing the aggregation of heterologous proteins in vitro, and this activity is preserved in various chimeras, even when these include coiled coils and OB domains from unrelated proteins. The structures suggest a molecular mechanism for substrate processing based on concerted radial motions of the coiled coils relative to the OB rings. Structure and activity of the N-terminal substrate recognition domains in proteasomal ATPases.,Djuranovic S, Hartmann MD, Habeck M, Ursinus A, Zwickl P, Martin J, Lupas AN, Zeth K Mol Cell. 2009 Jun 12;34(5):580-90. Epub 2009 May 28. PMID:19481487 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Gcn4

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