1z0v

Crystal Structure of A. fulgidus Lon proteolytic domain

spinqualitylabelsall models 1z0v, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1z0v is a 6 chain structure with sequence from Arcfl. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1z0t, 1z0g, 1z0e, 1z0b, 1z0c, 1z0w Activity: Endopeptidase La, with EC number 3.4.21.53 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [LONB_ARCFU] ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Degrades polypeptides processively (By similarity). 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 Although macromolecular crystallography is rapidly becoming largely routine owing to advances in methods of data collection, structure solution and refinement, difficult cases are still common. To remind structural biologists about the kinds of crystallographic difficulties that might be encountered, case studies of several successfully completed structure determinations that utilized less than perfect crystals are discussed here. The structure of the proteolytic domain of Archaeoglobus fulgidus Lon was solved with crystals that contained superimposed orthorhombic and monoclinic lattices, a case not previously described for proteins. Another hexagonal crystal form of this protein exhibited an unusually high degree of non-isomorphism. Crystals of A. fulgidus Rio1 kinase exhibited both pseudosymmetry and twinning. Ways of identifying the observed phenomena and approaches to solving and refining macromolecular structures when only less than perfect crystals are available are discussed here. Pathological crystallography: case studies of several unusual macromolecular crystals.,Dauter Z, Botos I, LaRonde-LeBlanc N, Wlodawer A Acta Crystallogr D Biol Crystallogr. 2005 Jul;61(Pt 7):967-75. Epub 2005, Jun 24. PMID:15983420 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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