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 pe glycosyltransferase domain with a typical Rossmann fold.

3 fold that differs sharply from the canonical 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 A subset of the proteins that adopt the Rossmann fold also bind to nucleotide cofactors such as

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

46 -2.3-A resolution and revealed an N-terminal Rossmann fold domain connected by a long alpha-helix to

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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