<table><tr><td colspan='2'>[[6hed]] is a 34 chain structure with sequence from [http://en.wikipedia.org/wiki/Arcfu Arcfu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HED OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HED FirstGlance]. <br>
<table><tr><td colspan='2'>[[6hed]] is a 34 chain structure with sequence from [http://en.wikipedia.org/wiki/Arcfu Arcfu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HED OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HED FirstGlance]. <br>
6hed is a 34 chain structure with sequence from Arcfu. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
[PSA_ARCFU] Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation (By similarity).[HAMAP-Rule:MF_00289_A] [PAN_ARCFU] ATPase which is responsible for recognizing, binding, unfolding and translocation of substrate proteins into the archaeal 20S proteasome core particle. Is essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C-termini of the proteasomal ATPase function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis. Unfolding activity requires energy from ATP hydrolysis, whereas ATP binding alone promotes ATPase-20S proteasome association which triggers gate opening, and supports translocation of unfolded substrates (Probable).[1] [PSB_ARCFU] Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation (By similarity).[HAMAP-Rule:MF_02113_A]
Publication Abstract from PubMed
Proteasomes occur in all three domains of life, and are the principal molecular machines for the regulated degradation of intracellular proteins. They play key roles in the maintenance of protein homeostasis, and control vital cellular processes. While the eukaryotic 26S proteasome is extensively characterized, its putative evolutionary precursor, the archaeal proteasome, remains poorly understood. The primordial archaeal proteasome consists of a 20S proteolytic core particle (CP), and an AAA-ATPase module. This minimal complex degrades protein unassisted by non-ATPase subunits that are present in a 26S proteasome regulatory particle (RP). Using cryo-EM single-particle analysis, we determined structures of the archaeal CP in complex with the AAA-ATPase PAN (proteasome-activating nucleotidase). Five conformational states were identified, elucidating the functional cycle of PAN, and its interaction with the CP. Coexisting nucleotide states, and correlated intersubunit signaling features, coordinate rotation of the PAN-ATPase staircase, and allosterically regulate N-domain motions and CP gate opening. These findings reveal the structural basis for a sequential around-the-ring ATPase cycle, which is likely conserved in AAA-ATPases.
Cryo-EM structures of the archaeal PAN-proteasome reveal an around-the-ring ATPase cycle.,Majumder P, Rudack T, Beck F, Danev R, Pfeifer G, Nagy I, Baumeister W Proc Natl Acad Sci U S A. 2018 Dec 17. pii: 1817752116. doi:, 10.1073/pnas.1817752116. PMID:30559193[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
↑ Djuranovic S, Hartmann MD, Habeck M, Ursinus A, Zwickl P, Martin J, Lupas AN, Zeth K. Structure and activity of the N-terminal substrate recognition domains in proteasomal ATPases. Mol Cell. 2009 Jun 12;34(5):580-90. Epub 2009 May 28. PMID:19481487 doi:10.1016/j.molcel.2009.04.030
↑ Majumder P, Rudack T, Beck F, Danev R, Pfeifer G, Nagy I, Baumeister W. Cryo-EM structures of the archaeal PAN-proteasome reveal an around-the-ring ATPase cycle. Proc Natl Acad Sci U S A. 2018 Dec 17. pii: 1817752116. doi:, 10.1073/pnas.1817752116. PMID:30559193 doi:http://dx.doi.org/10.1073/pnas.1817752116
