1vee

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NMR structure of the hypothetical rhodanese domain At4g01050 from Arabidopsis thalianaNMR structure of the hypothetical rhodanese domain At4g01050 from Arabidopsis thaliana

Structural highlights

1vee is a 1 chain structure with sequence from Arath. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:RIKEN CDNA RAFL06-68-J04 (ARATH)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

[STR4_ARATH] Rhodanese domain-containing protein required for anchoring ferredoxin--NADP reductase to the thylakoid membranes and sustaining efficient linear electron flow (LEF).[1]

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

The three-dimensional structure of the rhodanese homology domain At4g01050(175-195) from Arabidopsis thaliana has been determined by solution nuclear magnetic resonance methods based on 3043 upper distance limits derived from NOE intensities measured in three-dimensional NOESY spectra. The structure shows a backbone root mean square deviation to the mean coordinates of 0.43 A for the structured residues 7-125. The fold consists of a central parallel beta-sheet with five strands in the order 1-5-4-2-3 and arranged in the conventional counterclockwise twist, and helices packing against each side of the beta-sheet. Comparison with the sequences of other proteins with a rhodanese homology domain in Arabidopsis thaliana indicated residues that could play an important role in the scaffold of the rhodanese homology domain. Finally, a three-dimensional structure comparison of the present noncatalytic rhodanese homology domain with the noncatalytic rhodanese domains of sulfurtransferases from other organisms discloses differences in the length and conformation of loops that could throw light on the role of the noncatalytic rhodanese domain in sulfurtransferases.

Solution structure of the rhodanese homology domain At4g01050(175-295) from Arabidopsis thaliana.,Pantoja-Uceda D, Lopez-Mendez B, Koshiba S, Inoue M, Kigawa T, Terada T, Shirouzu M, Tanaka A, Seki M, Shinozaki K, Yokoyama S, Guntert P Protein Sci. 2005 Jan;14(1):224-30. Epub 2004 Dec 2. PMID:15576557[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Juric S, Hazler-Pilepic K, Tomasic A, Lepedus H, Jelicic B, Puthiyaveetil S, Bionda T, Vojta L, Allen JF, Schleiff E, Fulgosi H. Tethering of ferredoxin:NADP+ oxidoreductase to thylakoid membranes is mediated by novel chloroplast protein TROL. Plant J. 2009 Dec;60(5):783-94. doi: 10.1111/j.1365-313X.2009.03999.x. Epub 2009 , Aug 13. PMID:19682289 doi:http://dx.doi.org/10.1111/j.1365-313X.2009.03999.x
  2. Pantoja-Uceda D, Lopez-Mendez B, Koshiba S, Inoue M, Kigawa T, Terada T, Shirouzu M, Tanaka A, Seki M, Shinozaki K, Yokoyama S, Guntert P. Solution structure of the rhodanese homology domain At4g01050(175-295) from Arabidopsis thaliana. Protein Sci. 2005 Jan;14(1):224-30. Epub 2004 Dec 2. PMID:15576557 doi:10.1110/ps.041138705
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