1vjl: Difference between revisions

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[[Image:1vjl.gif|left|200px]]
[[Image:1vjl.gif|left|200px]]


{{Structure
<!--
|PDB= 1vjl |SIZE=350|CAPTION= <scene name='initialview01'>1vjl</scene>, resolution 1.90&Aring;
The line below this paragraph, containing "STRUCTURE_1vjl", creates the "Structure Box" on the page.
|SITE=
You may change the PDB parameter (which sets the PDB file loaded into the applet)
|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=UNL:UNKNOWN+LIGAND'>UNL</scene>
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|ACTIVITY=
or leave the SCENE parameter empty for the default display.
|GENE= TM0160 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 Thermotoga maritima])
-->
|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=COG1259 COG1259]</span>
{{STRUCTURE_1vjl| PDB=1vjl  | SCENE= }}  
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1vjl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vjl OCA], [http://www.ebi.ac.uk/pdbsum/1vjl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1vjl RCSB]</span>
}}


'''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'''
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==About this Structure==
==About this Structure==
1VJL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. This structure supersedes the now removed PDB entry 1O5Y. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VJL OCA].  
1VJL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1o5y 1o5y]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VJL OCA].  


==Reference==
==Reference==
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[[Category: Genomics, Joint Center for Structural.]]
[[Category: Genomics, Joint Center for Structural.]]
[[Category: JCSG, Joint Center for Structural Genomics.]]
[[Category: JCSG, Joint Center for Structural Genomics.]]
[[Category: jcsg]]
[[Category: Jcsg]]
[[Category: joint center for structural genomic]]
[[Category: Joint center for structural genomic]]
[[Category: predicted protein related to wound inducive proteins in plant]]
[[Category: Predicted protein related to wound inducive proteins in plant]]
[[Category: protein structure initiative]]
[[Category: Protein structure initiative]]
[[Category: psi]]
[[Category: Psi]]
[[Category: structural genomic]]
[[Category: Structural genomic]]
[[Category: tm0160]]
[[Category: Tm0160]]
 
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Revision as of 12:36, 3 May 2008

File:1vjl.gif

Template:STRUCTURE 1vjl

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. 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 Page seeded by OCA on Sat May 3 12:36:19 2008

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