ライフサイエンスコーパス: Rossmann fold

1 shown to occur in the NAD(+)-binding region (Rossmann fold).

2 fold that differs sharply from the canonical Rossmann fold.

3 pe glycosyltransferase domain with a typical Rossmann fold.

4 two other positively charged residues of the Rossmann fold.

5 ive-site structure whereas Trm5 features the Rossmann fold.

6 mosaic virus and a three-helix fragment of a Rossmann fold.

7 igins of coding as a property of the ancient Rossmann fold.

8 74-residue internal segment from within the Rossmann fold.

9 vel enzyme architecture that is built upon a Rossmann fold.

10 n of P5CR is an alpha/beta/alpha sandwich, a Rossmann fold.

11 The monomer fold is a highly conserved Rossmann fold.

12 f and an NADPH binding domain with a typical Rossmann fold.

13 eing novel and the C-terminal domain being a Rossmann fold.

14 an N-terminal domain that includes a typical Rossmann fold.

15 x interaction from the FAD or NAD(P)-binding Rossmann fold.

16 ow NmrA consists of two domains, including a Rossmann fold.

17 oducts are opposite from that expected for a Rossmann fold.

18 alpha-helices that exhibit the topology of a Rossmann fold.

19 ogy which is an interesting variation on the Rossmann-fold.

20 und NAD(P)H cofactor, which is embedded in a Rossmann-fold.

21 ude ancient folds such as the TIM-barrel and Rossmann folds.

22 denosylmethionine binding domain with a core Rossmann fold, a dimerization domain, a middle domain, a

23 ks the conserved eta2 3(10)-helix within the Rossmann fold, abolishing cofactor binding.

24 A subset of the proteins that adopt the Rossmann fold also bind to nucleotide cofactors such as

25 he amino terminus, followed by a gamma-class Rossmann fold amino-methyltransferase catalytic domain f

26 protein consists of a large domain having a Rossmann fold and a small domain containing a three-stra

27 The C-terminal domain contains a typical Rossmann fold and orients the dinucleotide.

28 central cavity between its CRISPR-associated Rossmann fold and restriction endonuclease domains that

29 The structure shows that SCO1815 adopts a Rossmann fold and suggests that a conformational change

30 iation of a sterile alpha motif domain and a Rossmann fold and that DprA forms tail-to-tail dimers.

31 ytic domain resembles a dinucleotide-binding Rossmann fold and the C-terminal domain adopts a left-ha

32 te significant structural similarity between Rossmann fold and TIM Barrel proteins, a link which is p

33 trate recognition common among both class I (Rossmann fold) and class II (SET domain) methyltransfera

34 f an N-terminal dinucleotide-binding domain (Rossmann-fold) and a C-terminal domain that contains a s

35 nclude a pyridine nucleotide-binding domain (Rossmann fold), and residues that might play key structu

36 a novel predicted nuclease of the Sir2-type Rossmann fold, and phosphatases of the HAD superfamily t

37 ps show that NAD(+) does not bind to the DUF Rossmann fold, and small-angle X-ray scattering reveals

38 at specific loop embellishments on the basic Rossmann fold are key determinants in the selection of t

39 Rossmann folds are ancient, frequently diverged domains

40 angstrom resolution showed that it adopts a Rossmann fold as do other characterized FabIs.

41 As expected, domain 1 shares the same Rossmann fold as the related enzymes, methionyl-tRNA-for

42 omer cooperates with several residues in the Rossmann fold as well as other regions of the other prot

43 These Rossmann folds can often be identified by the short amin

44 CRISPR-associated Rossmann Fold (CARF) and SMODS-associated and fused to v

45 tes Csm6 by binding to its CRISPR-associated Rossmann fold (CARF) domain.

46 ary Cas proteins harboring CRISPR-associated Rossmann fold (CARF) domains and regulate the activities

47 OA) messengers to activate CRISPR-associated Rossmann-fold (CARF) immune effectors.

48 ving the least structural elaboration of the Rossmann fold catalytic domain was the most specific, co

49 to that of cysteinyl-tRNA synthetase, with a Rossmann fold catalytic domain.

50 ights that the vast tRNA binding site of the Rossmann-fold catalytic domain of class I aminoacyl-tRNA

51 , and the associated rotational shift in the Rossmann fold closes the catalytic cleft with consequent

52 uman 3 beta-HSD/isomerase and identifies the Rossmann-fold coenzyme domain at the amino terminus.

53 ) on the opposite face with a characteristic Rossmann fold comprising two right-handed beta(1)alpha(1

54 he latter is unique to ALDH16 and features a Rossmann fold connected to a protruding beta-flap.

55 in containing the active-site tyrosine and a Rossmann fold containing several highly conserved acidic

56 lebrand factor type A-domain: an alpha/beta "Rossmann" fold containing a metal ion-dependent adhesion

57 e site is located at the C-terminal end of a Rossmann fold core, and three large insertions make sign

58 iable cap domain accessorizes the ubiquitous Rossmann-fold core domain.

59 The Rossmann fold domain binds to the terminus of the looser

60 -2.3-A resolution and revealed an N-terminal Rossmann fold domain connected by a long alpha-helix to

61 dopts a bilobal structure with an N-terminal Rossmann fold domain containing the N-10-formyltetrahydr

62 The structure contains a classic Rossmann fold domain in the N terminus and a small C-ter

63 posed of three domains: 1) an amino-terminal Rossmann fold domain that is responsible for formation o

64 tein fusion of the CP1 editing domain to the Rossmann fold domain that is ubiquitously found in kinas

65 ucture reveals the presence of an N-terminal Rossmann fold domain with a bound NAD(+) cofactor and a

66 ate defence enzymes with a CRISPR-associated Rossmann fold domain(6), sculpting a powerful antiviral

67 the active site cleft between the N-terminal Rossmann-fold domain and the C-terminal alpha-helical do

68 t undoubtedly corresponds to the N-terminal "Rossmann fold" domain, which has been proved to particip

69 having the signature sequence, comprises two Rossmann fold domains which bind coenzyme and substrate

70 g unconventional RNA-binding domains such as Rossmann-fold domains.

71 that bind associated CARF (CRISPR-Associated Rossmann Fold) domains.

72 ata indicate the divergence of several major Rossmann-fold enzyme classes, with different cofactors a

73 f the most widespread protein folds, such as Rossmann fold, ferredoxin fold, ribonuclease H fold, and

74 tructure as a scaffold predicted a classical Rossmann fold for the nucleotide binding, and an N-termi

75 This fold is highly reminiscent of the Rossmann fold, found in many NAD(P)H-dependent enzymes.

76 and-binding domain that adopts an alpha/beta Rossmann fold, has been proposed to allosterically regul

77 lpha/KMT9beta), belongs to the few described Rossmann-fold histone lysine methyltransferases and mono

78 Residue 522 lies within a Rossmann fold in the B' subfragment of topoisomerase II,

79 nsisting of a nonnative, partially assembled Rossmann fold, in the closed chamber of human chaperonin

80 structure for TM1088A shows a characteristic Rossmann fold indicating an NAD+ binding site and has st

81 on event splits the primary structure of the Rossmann fold into two halves.

82 The Rossmann fold is one of the most ancient and functionall

83 The Rossmann fold is one of the three most highly represente

84 The overall architecture featuring a Rossmann fold is topologically similar to that of deoxyr

85 don-binding domain and an insertion into the Rossmann-fold known as Connecting Peptide 1.

86 a-sheet surrounded by six alpha-helices in a Rossmann fold-like topology.

87 revealed a two-domain structure including a Rossmann-fold-like domain that constitutes a unique glyc

88 ue interactions between the cofactor and the Rossmann fold make isomerization possible while allowing

89 first emerged in bacteria and belongs to the Rossmann fold methyltransferase superfamily.

90 elongs to the S-adenosylmethionine-dependent Rossmann-fold methyltransferase superfamily and is relat

91 istance methyltransferases are SAM dependent Rossmann fold methyltransferases that convert A2058 of 2

92 the typical short-chain dehydrogenase (SDR) Rossmann-fold motif for nucleotide binding.

93 eyond CoA-binding sites and include abundant Rossmann-fold motifs that bind the ADP moiety of NADH, N

94 aoultella terrigena The beta-Kdo GT has dual Rossmann-fold motifs typical of GT-B enzymes, but extens

95 ket, which presents a fold distinct from the Rossmann fold observed in most known MTases.

96 The Rossmann fold of the catalytic core presents inducible a

97 -terminal domain rather than the anticipated Rossmann fold of the N-terminal domain.

98 -terminal alpha-helix of one subunit and the Rossmann folds of both subunits, thus affecting a specif

99 he specificity of NADH-OH towards the unique Rossmann-fold of complex I and indicates a regulatory ro

100 We see NADPH bound to the Rossmann fold, over 25 A from the previously proposed si

101 is caused by local perturbations within the Rossmann fold, possibly interfering with the bending of

102 lexity so that, even for the extremely large Rossmann fold protein class, results were obtained in ab

103 ng strategies can be successfully applied to Rossmann-fold protein methyltransferases.

104 cient and previously undescribed subclass of Rossmann-fold proteins that includes bacterial ornithine

105 ique positions, not commonly conserved among Rossmann-fold proteins, composing a well-conserved salt

106 enzyme, and each monomer possesses a typical Rossmann-fold structure.

107 subunits, which belong to the NAD(P)-binding Rossmann-fold superfamily.

108 of the class I fold, similar to the ancient Rossmann fold that binds nucleotides.

109 he oligomeric interface and (ii) a canonical Rossmann fold that interacts with a single dinucleotide

110 nce that in addition to this sequence motif, Rossmann folds that bind FAD and NAD(P) also typically c

111 dicative than previously described motifs of Rossmann folds that bind FAD or NAD(P).

112 These two motifs appear to stabilize the Rossmann fold: the first glycyl residue of either the GX

113 hough both are, to some extent, based on the Rossmann fold, their tertiary and quaternary structures

114 ain insert, reflecting the robustness of the Rossmann fold to mutation.

115 Fms1 consists of an FAD-binding domain, with Rossmann fold topology, and a substrate-binding domain.

116 The RCK domain has a Rossmann-fold topology with unique positions, not common

117 Each monomer adopts the Rossmann fold typical for many SAM-binding methyltransfe