1vjl | pdb_00001vjl

Crystal structure of a duf151 family protein (tm0160) from thermotoga maritima at 1.90 A resolution

spinqualitylabelsall models 1vjl, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1vjl is a 2 chain structure with sequence from Thermotoga maritima. This structure supersedes the now removed PDB entry 1o5y. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL, MSE, UNL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN Function Q9WY07_THEMA 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 The structure of two Thermotoga maritima proteins, a conserved hypothetical protein (TM0160) and a transcriptional regulator (TM1171), have now been determined at 1.9 A and 2.3 A resolution, respectively, as part of a large-scale structural genomics project. Our first efforts to crystallize full-length versions of these targets were unsuccessful. However, analysis of the recombinant purified proteins using the technique of enhanced amide hydrogen/deuterium exchange mass spectroscopy (DXMS) revealed substantial regions of rapid amide deuterium hydrogen exchange, consistent with flexible regions of the structures. Based on these exchange data, truncations were designed to selectively remove the disordered C-terminal regions, and the resulting daughter proteins showed greatly enhanced crystallizability. Comparative DXMS analysis of full-length protein versus truncated forms demonstrated complete and exact preservation of the exchange rate profiles in the retained sequence, indicative of conservation of the native folded structure. This study presents the first structures produced with the aid of the DXMS method for salvaging intractable crystallization targets. The structure of TM0160 represents a new fold and highlights the use of this approach where any prior structural knowledge is absent. The structure of TM1171 represents an example where the lack of a substrate/cofactor may impair crystallization. The details of both structures are presented and discussed. On the use of DXMS to produce more crystallizable proteins: structures of the T. maritima proteins TM0160 and TM1171.,Spraggon G, Pantazatos D, Klock HE, Wilson IA, Woods VL Jr, Lesley SA Protein Sci. 2004 Dec;13(12):3187-99. PMID:15557262 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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