ROS, Moss, and a Rossmann Fold Protein: Identification of a Key Signaling Component for Plant Immunity by Amelia H. Lovelace

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Putative NAD(P)-Binding Rossmann Fold Protein Is Involved in Chitosan-Induced Peroxidase Activity and Lipoxygenase Expression in Physcomitrium patens by Eeva M. Marttinen, Eva L. Decker, Petra Heinonen, Ralf Reski, Jari P. T. Valkonen

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The RNA repair proteins RtcAB regulate transcription activator RtcR via its CRISPR-associated Rossmann fold domain by Ioly Kotta-Loizou, Maria Grazia Giuliano, Milija Jovanovic, Jorrit Schaefer, Fuzhou Ye, Nan Zhang, Danai Athina Irakleidi, Xiaojiao Liu, Xiaodong Zhang, Martin Buck, Christoph Engl

“…Summary: CRISPR-associated Rossmann fold (CARF) domain signaling underpins modulation of CRISPR-Cas nucleases; however, the RtcR CARF domain controls expression of two conserved RNA repair enzymes, cyclase RtcA and ligase RtcB. …”
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<i>S</i>-adenosyl-<span style="font-variant: small-caps">l</span>-homocysteine Hydrolase: A Structural Perspective on the Enzyme with Two Rossmann-Fold Domains by Krzysztof Brzezinski

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Biosynthesis of the Pseudomonas aeruginosa Extracellular Polysaccharides, Alginate, Pel, and Psl. by Michael J Franklin, David E Nivens, Joel T Weadge, P Lynne Howell, P Lynne Howell

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Methyltransferases of <i>Riboviria</i> by Arcady Mushegian

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Enhanced Resistance of <i>atnigr1</i> against <i>Pseudomonas syringae</i> pv. <i>tomato</i> Suggests Negative Regulation of Plant Basal Defense and Systemic Acquired Resistance by <i>AtNIGR1</i> Encoding NAD(P)-Binding Rossmann-Fold in <i>Arabidopsis thaliana</i> by Tiba Nazar Al Azzawi, Murtaza Khan, Bong-Gyu Mun, Sang-Uk Lee, Muhammad Imran, Adil Hussain, Nkulu Kabange Rolly, Da-Sol Lee, Sajid Ali, In-Jung Lee, Byung-Wook Yun

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A redox‐active HybG‐HypD scaffold complex is required for optimal ATPase activity during [NiFe]‐hydrogenase maturation in Escherichia coli by Alexander Haase, R. Gary Sawers

“…Two conserved cysteine residues, C69 and C72, form part of HypD's Rossmann fold and play a role in HypD's thiol‐disulfide exchange activity. …”
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The human sirtuin family: Evolutionary divergences and functions by Vassilopoulos Athanassios, Fritz Kristofer S, Petersen Dennis R, Gius David

“…The highly conserved catalytic core domain composed of a large oxidised nicotinamide adenine dinucleotide (NAD⁺)-binding Rossmann fold subunit suggests that these proteins belong to a family of nutrient-sensing regulators. …”
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The cardiomyocyte RNA-binding proteome: Links to intermediary metabolism and heart disease by Castello Palomares, A, Liao, Y, Fischer, B, Leicht, S, Föehr, S, Frese, C, Ragan, C, Kurscheid, S, Pagler, E, Yang, H, Krijgsveld, J, Hentze, M, Preiss, T

“…RNA-enzyme contacts frequently involve Rossmann fold domains with examples in evidence of both,mutual exclusivity of, or compatibility between RNA binding and enzymatic function. …”

Short-chain dehydrogenases/reductases (SDR): the 2002 update. by Oppermann, U, Filling, C, Hult, M, Shafqat, N, Wu, X, Lindh, M, Shafqat, J, Nordling, E, Kallberg, Y, Persson, B, Jörnvall, H

“…Despite low sequence identities between different forms (about 15-30%), the 3D structures display highly similar alpha/beta folding patterns with a central beta-sheet, typical of the Rossmann-fold. Based on distinct sequence motifs functional assignments and classifications are possible, making it possible to build a general nomenclature system. …”

The crystal structure of E. coli pantothenate synthetase confirms it as a member of the cytidylyltransferase superfamily. by von Delft, F, Lewendon, A, Dhanaraj, V, Blundell, T, Abell, C, Smith, A

“…The enzyme is dimeric, with two well-defined domains per protomer: the N-terminal domain, a Rossmann fold, contains the active site cavity, with the C-terminal domain forming a hinged lid. …”

The cardiomyocyte RNA-binding proteome: links to intermediary metabolism and heart disease by Castello, A, Liao, Y, Fischer, B, Leicht, S, Föehr, S, Frese, C, Ragan, C, Kurscheid, S, Pagler, E, Yang, H, Krijgsveld, J, Hentze, M, Preiss, T

“…RNA-enzyme contacts frequently involve Rossmann fold domains with examples in evidence of both, mutual exclusivity of, or compatibility between RNA binding and enzymatic function. …”

The crystal structure of shikimate dehydrogenase (AroE) reveals a unique NADPH binding mode. by Ye, S, von Delft, F, Brooun, A, Knuth, M, Swanson, R, McRee, D

“…The molecule contains two domains, a catalytic domain with a novel open twisted alpha/beta motif and an NADPH binding domain with a typical Rossmann fold. The enzyme contains a unique glycine-rich P-loop with a conserved sequence motif, GAGGXX, that results in NADPH adopting a nonstandard binding mode with the nicotinamide and ribose moieties disordered in the binary complex. …”

Features of Protein Unfolding Transitions and Their Relation to Domain Topology Probed by Single-Molecule FRET by Nuno Bustorff, Jörg Fitter

“…Based on the structural homology of the domains (characterized by a Rossmann fold) and the striking similarity in the features of the measured distance changes during unfolding, clear evidence emerged that the underlying domain topology plays an important role in determining the observed structural changes.…”
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Metabolic Functions of Biliverdin IXβ Reductase in Redox-Regulated Hematopoietic Cell Fate by Wadie F. Bahou, Natalia Marchenko, Natasha M. Nesbitt

“…BLVRB crystallographic and thermodynamic studies have elucidated critical determinants of substrate utilization, redox coupling and cytoprotection, and have established that inhibitors and substrates bind within the single-Rossmann fold. These advances provide unique opportunities for the development of BLVRB-selective redox inhibitors as novel cellular targets that retain potential for therapeutic applicability in hematopoietic (and other) disorders.…”
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Structural and biochemical characterization of human orphan DHRS10 reveals a novel cytosolic enzyme with steroid dehydrogenase activity. by Lukacik, P, Keller, B, Bunkoczi, G, Kavanagh, K, Kavanagh, K, Lee, W, Hwa Lee, W, Adamski, J, Oppermann, U

“…The crystal structure of the DHRS10 apoenzyme exhibits secondary structure of the SDR (short-chain dehydrogenase/reductase) family: a Rossmann-fold with variable loops surrounding the active site. …”

The structure of the negative transcriptional regulator NmrA reveals a structural superfamily which includes the short-chain dehydrogenase/reductases. by Stammers, D, Ren, J, Leslie, K, Nichols, C, Lamb, H, Cocklin, S, Dodds, A, Hawkins, A

“…X-ray structures of two NmrA crystal forms, both to 1.8 A resolution, show NmrA consists of two domains, including a Rossmann fold. NmrA shows an unexpected similarity to the short-chain dehydrogenase/reductase (SDR) family, with the closest relationship to UDP-galactose 4-epimerase. …”

Structural and mechanistic themes in glycoconjugate biosynthesis at membrane interfaces by Allen, Karen N, Imperiali, Barbara

“…Lipid A biosynthesis enzymes illustrate that variations on the robust Rossmann fold allow substrate diversity. Improved understanding of GT and PGT structure and function holds promise for better function prediction and improvement of therapeutic inhibitory ligands.…”
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Clavulanic acid dehydrogenase: structural and biochemical analysis of the final step in the biosynthesis of the beta-lactamase inhibitor clavulanic acid. by MacKenzie, A, Kershaw, N, Hernandez, H, Robinson, C, Schofield, C, Andersson, I

“…The structure reveals that the individual monomers comprise a single domain possessing the Rossmann fold, characteristic of dinucleotide-binding enzymes. …”