3sbb

Disulphide-mediated Tetramer of T4 Lysozyme R76C/R80C by Synthetic SymmetrizationDisulphide-mediated Tetramer of T4 Lysozyme R76C/R80C by Synthetic Symmetrization

Structural highlights 3sbb is a 1 chain structure with sequence from Escherichia virus T4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.434Å Ligands: Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ENLYS_BPT4 Endolysin with lysozyme activity that degrades host peptidoglycans and participates with the holin and spanin proteins in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles. Once the holin has permeabilized the host cell membrane, the endolysin can reach the periplasm and break down the peptidoglycan layer. Publication Abstract from PubMed Combining the concepts of synthetic symmetrization with the approach of engineering metal binding sites, we have developed a new crystallization methodology termed metal-mediated synthetic symmetrization. In this method, pairs of histidine or cysteine mutations are introduced on the surface of target proteins, generating crystal lattice contacts or oligomeric assemblies upon coordination with metal. Metal-mediated synthetic symmetrization greatly expands the packing and oligomeric assembly possibilities of target proteins, thereby increasing the chances of growing diffraction-quality crystals. To demonstrate this method, we designed various T4 lysozyme (T4L) and maltose-binding protein (MBP) mutants and co-crystallized them with one of three metal ions: copper (Cu(2+) ), nickel (Ni(2+) ) or zinc (Zn(2+) ). The approach resulted in 16 new crystal structures - 8 for T4L and 8 for MBP - displaying a variety of oligomeric assemblies and packing modes, representing in total 13 new and distinct crystal forms for these proteins. We discuss the potential utility of the method for crystallizing target proteins of unknown structure by engineering in pairs of histidine or cysteine residues. As an alternate strategy, we propose that the varied crystallization-prone forms of T4L or MBP engineered in this work could be used as crystallization chaperones, by fusing them genetically to target proteins of interest. An approach to crystallizing proteins by metal-mediated synthetic symmetrization.,Laganowsky A, Zhao M, Soriaga AB, Sawaya MR, Cascio D, Yeates TO Protein Sci. 2011 Sep 6. doi: 10.1002/pro.727. PMID:21898649 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Lysozyme 3D structures

spinqualitylabelsall models 3sbb, resolution 1.43Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image