4ypl | pdb_00004ypl

Crystal structure of a hexameric LonA protease bound to three ADPs

spinqualitylabelsall models 4ypl, resolution 3.45Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4ypl is a 6 chain structure with sequence from Meiothermus taiwanensis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.45Å Ligands: 4KZ, ADP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A059VAZ3_9DEIN ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.[HAMAP-Rule:MF_01973] Publication Abstract from PubMed The Lon AAA+ protease (LonA) is an evolutionarily conserved protease that couples the ATPase cycle into motion to drive substrate translocation and degradation. A hallmark feature shared by AAA+ proteases is the stimulation of ATPase activity by substrates. Here we report the structure of LonA bound to three ADPs, revealing the first AAA+ protease assembly where the six protomers are arranged alternately in nucleotide-free and bound states. Nucleotide binding induces large coordinated movements of conserved pore loops from two pairs of three non-adjacent protomers and shuttling of the proteolytic groove between the ATPase site and a previously unknown Arg paddle. Structural and biochemical evidence supports the roles of the substrate-bound proteolytic groove in allosteric stimulation of ATPase activity and the conserved Arg paddle in driving substrate degradation. Altogether, this work provides a molecular framework for understanding how ATP-dependent chemomechanical movements drive allosteric processes for substrate degradation in a major protein-destruction machine. Structural Insights into the Allosteric Operation of the Lon AAA+ Protease.,Lin CC, Su SC, Su MY, Liang PH, Feng CC, Wu SH, Chang CI Structure. 2016 May 3;24(5):667-75. doi: 10.1016/j.str.2016.03.001. Epub 2016 Mar, 31. PMID:27041592 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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