1vjl: Difference between revisions

Revision as of 07:09, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1vjl.png

Template:STRUCTURE 1vjl

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

Template:ABSTRACT PUBMED 15557262

About this StructureAbout this Structure

1VJL is a Single protein structure of sequence from Thermotoga maritima. This structure supersedes 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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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''CRYSTAL STRUCTURE OF PREDICTED PROTEIN RELATED TO WOUND INDUCIVE PROTEINS IN PLANTS (TM0160) FROM THERMOTOGA MARITIMA AT 1.90 A RESOLUTION'''
+===CRYSTAL STRUCTURE OF PREDICTED PROTEIN RELATED TO WOUND INDUCIVE PROTEINS IN PLANTS (TM0160) FROM THERMOTOGA MARITIMA AT 1.90 A RESOLUTION===
-==Overview==
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-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.
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+{{ABSTRACT_PUBMED_15557262}}
 ==About this Structure==
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 [[Category: Structural genomic]]
 [[Category: Tm0160]]
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