1fh1

BACKBONE FOLD OF NODF

spinqualitylabelsall models 1fh1, 1 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1fh1 is a 1 chain structure with sequence from "bacillus_francki"_matzuschita_1902 "bacillus francki" matzuschita 1902. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [NODF_RHILV] Proposed to synthesize nod factor fatty acyl chain. Involved in trans-2,trans-4,trans-6,cis-11-octadecatetraenoic acid biosynthesis. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Over the next few years, various genome projects will sequence many new genes and yield many new gene products. Many of these products will have no known function and little, if any, sequence homology to existing proteins. There is reason to believe that a rapid determination of a protein fold, even at low resolution, can aid in the identification of function and expedite the determination of structure at higher resolution. Recently devised NMR methods of measuring residual dipolar couplings provide one route to the determination of a fold. They do this by allowing the alignment of previously identified secondary structural elements with respect to each other. When combined with constraints involving loops connecting elements or other short-range experimental distance information, a fold is produced. We illustrate this approach to protein fold determination on (15)N-labeled Eschericia coli acyl carrier protein using a limited set of (15)N-(1)H and (1)H-(1)H dipolar couplings. We also illustrate an approach using a more extended set of heteronuclear couplings on a related protein, (13)C, (15)N-labeled NodF protein from Rhizobium leguminosarum. Rapid determination of protein folds using residual dipolar couplings.,Fowler CA, Tian F, Al-Hashimi HM, Prestegard JH J Mol Biol. 2000 Dec 1;304(3):447-60. PMID:11090286 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also NodS

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