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7AKR

Human ADP-ribosylserine hydrolase ARH3 mutant E41A in complex with ADP-ribose dimer

This is a non-PDB format compatible entry.
Summary for 7AKR
Entry DOI10.2210/pdb7akr/pdb
DescriptorADP-ribose glycohydrolase ARH3, MAGNESIUM ION, [(2R,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-3,4-DIHYDROXY-OXOLAN-2-YL]METHYL [HYDROXY-[[(2R,3S,4R,5S)-3,4,5-TRIHYDROXYOXOLAN-2-YL]METHOXY]PHOSPHORYL] HYDROGEN PHOSPHATE, ... (6 entities in total)
Functional Keywordsadp-ribosylation, adp-ribose, adprhl2, adp-ribosylhydrolase like 2, ser-adpr, serine-adpr, hydrolase
Biological sourceHomo sapiens (Human)
Total number of polymer chains4
Total formula weight157042.15
Authors
Ariza, A. (deposition date: 2020-10-02, release date: 2021-06-16, Last modification date: 2024-10-23)
Primary citationRack, J.G.M.,Liu, Q.,Zorzini, V.,Voorneveld, J.,Ariza, A.,Honarmand Ebrahimi, K.,Reber, J.M.,Krassnig, S.C.,Ahel, D.,van der Marel, G.A.,Mangerich, A.,McCullagh, J.S.O.,Filippov, D.V.,Ahel, I.
Mechanistic insights into the three steps of poly(ADP-ribosylation) reversal.
Nat Commun, 12:4581-4581, 2021
Cited by
PubMed Abstract: Poly(ADP-ribosyl)ation (PAR) is a versatile and complex posttranslational modification composed of repeating units of ADP-ribose arranged into linear or branched polymers. This scaffold is linked to the regulation of many of cellular processes including the DNA damage response, alteration of chromatin structure and Wnt signalling. Despite decades of research, the principles and mechanisms underlying all steps of PAR removal remain actively studied. In this work, we synthesise well-defined PAR branch point molecules and demonstrate that PARG, but not ARH3, can resolve this distinct PAR architecture. Structural analysis of ARH3 in complex with dimeric ADP-ribose as well as an ADP-ribosylated peptide reveal the molecular basis for the hydrolysis of linear and terminal ADP-ribose linkages. We find that ARH3-dependent hydrolysis requires both rearrangement of a catalytic glutamate and induction of an unusual, square-pyramidal magnesium coordination geometry.
PubMed: 34321462
DOI: 10.1038/s41467-021-24723-3
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.95 Å)
Structure validation

231029

數據於2025-02-05公開中

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