7qsu

Crystal structure of homing endonuclease-associated TliVMA intein (C1A, d333-339)

spinqualitylabelsall models 7qsu, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7qsu is a 1 chain structure with sequence from Thermococcus litoralis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.9Å Ligands: EPE, MPD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function H3ZKG9_THELN Produces ATP from ADP in the presence of a proton gradient across the membrane. The archaeal alpha chain is a catalytic subunit.[ARBA:ARBA00003912][HAMAP-Rule:MF_00309] Publication Abstract from PubMed Inteins catalyze their removal from a host protein through protein splicing. Inteins that contain an additional site-specific endonuclease domain display genetic mobility via a process termed "homing" and thereby act as selfish DNA elements. We elucidated the crystal structures of two archaeal inteins associated with an active or inactive homing endonuclease domain. This analysis illustrated structural diversity in the accessory domains (ACDs) associated with the homing endonuclease domain. To augment homing endonucleases with highly specific DNA cleaving activity using the intein scaffold, we engineered the ACDs and characterized their homing site recognition. Protein engineering of the ACDs in the inteins illuminated a possible strategy for how inteins could avoid their extinction but spread via the acquisition of a diverse accessory domain. Structural Basis for the Propagation of Homing Endonuclease-Associated Inteins.,Beyer HM, Iwai H Front Mol Biosci. 2022 Mar 16;9:855511. doi: 10.3389/fmolb.2022.855511., eCollection 2022. PMID:35372505 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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