1vjl

File:1vjl.gif

spinqualitylabelsall models 1vjl, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL STRUCTURE OF PREDICTED PROTEIN RELATED TO WOUND INDUCIVE PROTEINS IN PLANTS (TM0160) FROM THERMOTOGA MARITIMA AT 1.90 A RESOLUTION

OverviewOverview

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.

About this StructureAbout this Structure

1VJL is a Single protein structure of sequence from Thermotoga maritima with CL and UNL as ligands. This structure superseeds the now removed PDB entry 1O5Y. Full crystallographic information is available from OCA.

ReferenceReference

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

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