WordNet

bend or lay so that one part covers the other; "fold up the newspaper"; "turn up your collar" (同)fold up, turn up
an angular or rounded shape made by folding; "a fold in the napkin"; "a crease in his trousers"; "a plication on her blouse"; "a flexure of the colon"; "a bend of his elbow" (同)crease, plication, flexure, crimp, bend
a geological process that causes a bend in a stratum of rock (同)folding
incorporate a food ingredient into a mixture by repeatedly turning it over without stirring or beating; "Fold the egg whites into the batter"
the act of folding; "he gave the napkins a double fold" (同)folding
a pen for sheep (同)sheepfold, sheep pen, sheepcote
a folded part (as in skin or muscle) (同)plica
become folded or folded up; "The bed folds in a jiffy" (同)fold up

PrepTutorEJDIC

《副語[句]を伴って》〈紙など〉‘を'『折る』,折り重ねる / 〈両手など〉‘を'『組む』;〈鳥が〉〈翼〉‘を'畳む / (…に)…‘を'巻き付ける《+『around(about)』+『名』》 / …‘を'抱き締める(embrace) / 《副語[句]を伴って》〈扇などが〉折リ畳める / 《話》〈事業などが〉つぶれる,閉じる《+『up』》 / ひだ / 折り目,畳み目 / (土地の)くぼみ / 起伏
(家畜,特に羊を入れておく)囲い,おり / 《比喩(ひゆ)的に》キリスト教会
折り畳みの

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2012/11/26 01:31:47」(JST)

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An example of the Rossmann fold, a structural domain of a decarboxylase protein from the bacterium Staphylococcus epidermidis (PDB ID 1G5Q) with the bound flavin mononucleotide cofactor shown.

The Rossmann fold is a protein structural motif found in proteins that bind nucleotides, especially the cofactor NAD. The structure with two repeats is composed of six parallel beta strands linked to two pairs of alpha helices in the topological order beta-alpha-beta-alpha-beta. Because each Rossmann fold can bind one nucleotide, binding domains for dinucleotides such as NAD consist of two paired Rossmann folds that each bind one nucleotide moiety of the cofactor molecule. Single Rossmann folds can bind mononucleotides such as the cofactor FMN.

The motif is named for Michael Rossmann, who first pointed out that this is a frequently occurring motif in nucleotide binding proteins, such as dehydrogenases.^[1]

In 1989, Israel Hanukoglu from the Weizmann Institute of Science discovered that the consensus sequence for NADP binding site in some enzymes that utilize NADP differs from the NAD binding motif.^[2] This discovery was used to re-engineer coenzyme specificities of enzymes.^[3]

References

^ Rao S, Rossmann M (1973). "Comparison of super-secondary structures in proteins". J Mol Biol 76 (2): 241–56. doi:10.1016/0022-2836(73)90388-4. PMID 4737475.
^ Hanukoglu, I.; Gutfinger, T. (Mar 1989). "cDNA sequence of adrenodoxin reductase. Identification of NADP-binding sites in oxidoreductases.". Eur J Biochem 180 (2): 479-84. doi:10.1111/j.1432-1033.1989.tb14671.x. PMID 2924777. http://onlinelibrary.wiley.com/doi/10.1111/j.1432-1033.1989.tb14671.x/pdf.
^ Scrutton NS, Berry A, Perham RN (January 1990). "Redesign of the coenzyme specificity of a dehydrogenase by protein engineering.". Nature 343 (6253): 38-43. doi:10.1038/343038a0. PMID 2296288.

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English Journal

Helicobacter pylori periplasmic receptor CeuE (HP1561) modulates its nickel affinity via organic metallophores.

Shaik MM, Cendron L, Salamina M, Ruzzene M, Zanotti G.Author information Department of Biomedical Sciences, University of Padua, Viale G. Colombo 3, 35131 Padua, Italy.AbstractIn Gram-negative bacteria, nickel uptake is guaranteed by multiple and complex systems that operate at the membrane and periplasmic level. H. pylori employs other yet uncharacterized systems to import the nickel required for the maturation of key enzymes, such as urease and hydrogenase. H. pylori CeuE protein (HP1561), previously annotated as the periplasmic component of an ABC-type transporter apparatus responsible of heme/siderophores or other Fe(III)-complexes uptake, has been recently proposed to be on the contrary involved in nickel/cobalt acquisition. In this work, the crystal structure of H. pylori CeuE has been determined at 1.65Å resolution using the SAD method. It comprises two structurally similar globular domains, each consisting of a central five-stranded β-sheet surrounded by α-helices, an arrangement commonly classified as a Rossmann-like fold. Structurally, H. pylori CeuE belongs to the class III periplasmic substrate-binding protein. Both crystallographic data and fluorescence binding assays allow to exclude a role of the protein in the transport of Vitamin B12, enterobactin, heme and isolated Ni2+ ions. On the contrary, the crystal structure and plasmon resonance studies about CeuE/Ni-(L-His)2 complex indicate that in H. pylori nickel transport is supported by CeuE protein and requires the presence of a natural nickelophore, analogously to what has been recently demonstrated for NikA from E.coli.
Molecular microbiology.Mol Microbiol.2013 Dec 12. doi: 10.1111/mmi.12487. [Epub ahead of print]
In Gram-negative bacteria, nickel uptake is guaranteed by multiple and complex systems that operate at the membrane and periplasmic level. H. pylori employs other yet uncharacterized systems to import the nickel required for the maturation of key enzymes, such as urease and hydrogenase. H. pylori Ce
PMID 24330328

Identification of novel methyltransferases, Bmt5 and Bmt6, responsible for the m3U methylations of 25S rRNA in Saccharomyces cerevisiae.

Sharma S, Yang J, Düttmann S, Watzinger P, Kötter P, Entian KD.Author information Department of Molecular Genetics and Cellular Microbiology, Institute of Molecular Biosciences, Goethe University, Frankfurt, Max-von-Laue Strasse 9, Frankfurt/M 60438, Germany.AbstractRNA contains various chemical modifications that expand its otherwise limited repertoire to mediate complex processes like translation and gene regulation. 25S rRNA of the large subunit of ribosome contains eight base methylations. Except for the methylation of uridine residues, methyltransferases for all other known base methylations have been recently identified. Here we report the identification of BMT5 (YIL096C) and BMT6 (YLR063W), two previously uncharacterized genes, to be responsible for m3U2634 and m3U2843 methylation of the 25S rRNA, respectively. These genes were identified by RP-HPLC screening of all deletion mutants of putative RNA methyltransferases and were confirmed by gene complementation and phenotypic characterization. Both proteins belong to Rossmann-fold-like methyltransferases and the point mutations in the S-adenosyl-l-methionine binding pocket abolish the methylation reaction. Bmt5 localizes in the nucleolus, whereas Bmt6 is localized predominantly in the cytoplasm. Furthermore, we showed that 25S rRNA of yeast does not contain any m5U residues as previously predicted. With Bmt5 and Bmt6, all base methyltransferases of the 25S rRNA have been identified. This will facilitate the analyses of the significance of these modifications in ribosome function and cellular physiology.
Nucleic acids research.Nucleic Acids Res.2013 Dec 11. [Epub ahead of print]
RNA contains various chemical modifications that expand its otherwise limited repertoire to mediate complex processes like translation and gene regulation. 25S rRNA of the large subunit of ribosome contains eight base methylations. Except for the methylation of uridine residues, methyltransferases f
PMID 24335083

Rubella virus capsid protein structure and its role in virus assembly and infection.

Mangala Prasad V, Willows SD, Fokine A, Battisti AJ, Sun S, Plevka P, Hobman TC, Rossmann MG.Author information Department of Biological Sciences, Purdue University, West Lafayette, IN 47907.AbstractRubella virus (RV) is a leading cause of birth defects due to infectious agents. When contracted during pregnancy, RV infection leads to severe damage in fetuses. Despite its medical importance, compared with the related alphaviruses, very little is known about the structure of RV. The RV capsid protein is an essential structural component of virions as well as a key factor in virus-host interactions. Here we describe three crystal structures of the structural domain of the RV capsid protein. The polypeptide fold of the RV capsid protomer has not been observed previously. Combining the atomic structure of the RV capsid protein with the cryoelectron tomograms of RV particles established a low-resolution structure of the virion. Mutational studies based on this structure confirmed the role of amino acid residues in the capsid that function in the assembly of infectious virions.
Proceedings of the National Academy of Sciences of the United States of America.Proc Natl Acad Sci U S A.2013 Dec 10;110(50):20105-10. doi: 10.1073/pnas.1316681110. Epub 2013 Nov 26.
Rubella virus (RV) is a leading cause of birth defects due to infectious agents. When contracted during pregnancy, RV infection leads to severe damage in fetuses. Despite its medical importance, compared with the related alphaviruses, very little is known about the structure of RV. The RV capsid pro
PMID 24282305

Japanese Journal

パーキンソン病関連タンパク質DJ-1の結晶構造解析

本坊和也,鈴木展生,稲垣冬彦
日本結晶学会誌 47(6), 390-395, 2005-12-27
… DJ-1 forms a dimer in the crystal, and the monomer takes a flavodoxin-like Rossmann-fold. …
NAID 10016908477

A New Family of NAD(P)H-Dependent Oxidoreductases Distinct from Conventional Rossmann-Fold Proteins

Muramatsu Hisashi,Mihara Hisaaki,Goto Masaru [他],MIYAHARA IKUKO,HIROTSU KEN,KURIHARA TATSUO,ESAKI NOBUYOSHI
Journal of bioscience and bioengineering 99(6), 541-547, 2005-06-25
… A new family of NAD(P)H-dependent oxidoreductases is now recognized as a protein family distinct from conventional Rossmann-fold proteins. …
NAID 110002695699

タンパク質三次元共通構造特徴の自動認識

加藤博明,高橋由雅
The Journal of chemical software 7(4), 161-170, 2001-12-01
… The program, called AIM (Automated Identification of 3D Motif of proteins), was developed and tested by computational experiments in searching for the secondary structure segments related to the Rossmann-fold motif as a 3D common structural feature between <I>alcohol dehydrogenase</I> …
NAID 10007641656