1vjl
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1vjl.gif|left|200px]] | + | [[Image:1vjl.gif|left|200px]] |
| - | + | ||
| - | '''CRYSTAL STRUCTURE OF PREDICTED PROTEIN RELATED TO WOUND INDUCIVE PROTEINS IN PLANTS (TM0160) FROM THERMOTOGA MARITIMA AT 1.90 A RESOLUTION''' | + | {{Structure |
| + | |PDB= 1vjl |SIZE=350|CAPTION= <scene name='initialview01'>1vjl</scene>, resolution 1.90Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> and <scene name='pdbligand=UNL:'>UNL</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= TM0160 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 Thermotoga maritima]) | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF PREDICTED PROTEIN RELATED TO WOUND INDUCIVE PROTEINS IN PLANTS (TM0160) FROM THERMOTOGA MARITIMA AT 1.90 A RESOLUTION''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1VJL is a [ | + | 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]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15557262 15557262] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Thermotoga maritima]] | [[Category: Thermotoga maritima]] | ||
| Line 18: | Line 27: | ||
[[Category: UNL]] | [[Category: UNL]] | ||
[[Category: jcsg]] | [[Category: jcsg]] | ||
| - | [[Category: joint center for structural | + | [[Category: joint center for structural genomic]] |
| - | [[Category: predicted protein related to wound inducive proteins in | + | [[Category: predicted protein related to wound inducive proteins in plant]] |
[[Category: protein structure initiative]] | [[Category: protein structure initiative]] | ||
[[Category: psi]] | [[Category: psi]] | ||
| - | [[Category: structural | + | [[Category: structural genomic]] |
[[Category: tm0160]] | [[Category: tm0160]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:46:29 2008'' |
Revision as of 12:46, 20 March 2008
| |||||||
| , resolution 1.90Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Gene: | TM0160 (Thermotoga maritima) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF PREDICTED PROTEIN RELATED TO WOUND INDUCIVE PROTEINS IN PLANTS (TM0160) FROM THERMOTOGA MARITIMA AT 1.90 A RESOLUTION
Overview
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 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.
Reference
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 Thu Mar 20 14:46:29 2008
Categories: Single protein | Thermotoga maritima | Genomics, Joint Center for Structural. | JCSG, Joint Center for Structural Genomics. | CL | UNL | Jcsg | Joint center for structural genomic | Predicted protein related to wound inducive proteins in plant | Protein structure initiative | Psi | Structural genomic | Tm0160
