1x9a
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam04077 DsrH]</span> | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1x9a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x9a OCA], [http://www.ebi.ac.uk/pdbsum/1x9a PDBsum], [http://www.fli-leibniz.de/cgi-bin/ImgLib.pl?CODE=1kfv JenaLib], [http://www.rcsb.org/pdb/explore.do?structureId=1x9a RCSB]</span> | ||
}} | }} | ||
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[[Category: structural genomic]] | [[Category: structural genomic]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 26 06:10:46 2008'' |
Revision as of 04:10, 26 March 2008
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| Domains: | DsrH | ||||||
| Resources: | FirstGlance, OCA, PDBsum, JenaLib, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Solution NMR Structure of Protein Tm0979 from Thermotoga maritima. Ontario Center for Structural Proteomics Target TM0979_1_87; Northeast Structural Genomics Consortium Target VT98.
Overview
We report herein the NMR structure of Tm0979, a structural proteomics target from Thermotoga maritima. The Tm0979 fold consists of four beta/alpha units, which form a central parallel beta-sheet with strand order 1234. The first three helices pack toward one face of the sheet and the fourth helix packs against the other face. The protein forms a dimer by adjacent parallel packing of the fourth helices sandwiched between the two beta-sheets. This fold is very interesting from several points of view. First, it represents the first structure determination for the DsrH family of conserved hypothetical proteins, which are involved in oxidation of intracellular sulfur but have no defined molecular function. Based on structure and sequence analysis, possible functions are discussed. Second, the fold of Tm0979 most closely resembles YchN-like folds; however the proteins that adopt these folds differ in secondary structural elements and quaternary structure. Comparison of these proteins provides insight into possible mechanisms of evolution of quaternary structure through a simple mechanism of hydrophobicity-changing mutations of one or two residues. Third, the Tm0979 fold is found to be similar to flavodoxin-like folds and beta/alpha barrel proteins, and may provide a link between these very abundant folds and putative ancestral half-barrel proteins.
About this Structure
1X9A is a Single protein structure of sequence from Thermotoga maritima. Full crystallographic information is available from OCA.
Reference
A novel member of the YchN-like fold: solution structure of the hypothetical protein Tm0979 from Thermotoga maritima., Gaspar JA, Liu C, Vassall KA, Meglei G, Stephen R, Stathopulos PB, Pineda-Lucena A, Wu B, Yee A, Arrowsmith CH, Meiering EM, Protein Sci. 2005 Jan;14(1):216-23. PMID:15608123
Page seeded by OCA on Wed Mar 26 06:10:46 2008
Categories: Single protein | Thermotoga maritima | Arrowsmith, C H. | Gaspar, J A. | Liu, C. | Meglei, G. | Meiering, E M. | NESG, Northeast Structural Genomics Consortium. | Pineda-Lucena, A. | Stathopulos, P B. | Stephen, R. | Vassall, K A. | Wu, B. | Yee, A. | Beta-alpha protein | Dimer | Hypothetical protein | Nesg | Northeast structural genomics consortium | Ocsp | Protein structure initiative | Psi | Structural genomic
