3set | pdb_00003set

Ni-mediated Dimer of Maltose-binding Protein A216H/K220H by Synthetic Symmetrization (Form I)

spinqualitylabelsall models 3set, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3set is a 2 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GLC, NI Related: 3ser, 3ses, 3seu, 3sev, 3sew, 3sex, 3sey Gene: b4034, JW3994, malE (ECOLI) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [MALE_ECOLI] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides. 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 Maltose-binding protein 3D structures

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