The Student Movement Volume 108 Issue 2: World Changers Assemble!

HUMANS Meet Pastor Taurus Montgomery, Colin Cha Uniting AULA with Sofia Oudri, Grace No World Changers Take On Changing the World, Savannah Tyler ARTS & ENTERTAINMENT Bewitched: An Album for the Fall Season, Lexie Dunham Music Notes for Change Day, Aiko J. Ayala Rios Processing Through Poetry: Raw & Real, Madison Vath NEWS Being Unstoppable: AU Fall Week of Prayer, Jonathan Clough FIBA Games Spark Questions for Competing Nations Ahead of the \u2724 Summer Olympics, Andrew Francis Honors\u27 Agape Feast Starts New Year of Faith and Fellowship, Andrew Francis IDEAS A Life Worth Living, Reagan Westerman The Victoria\u27s Secret Fashion Show Returns: Is it a Marketing Tactic or Genuine Change?, Daena Holbrook PULSE AU Sports, Alyssa Caruthers More Change Day Experiences, Various Students The Strange Thing About Service, Wambui Karanja Uplifting Spaces on Campus: Reflections from Nicole Compton-Gray, Nicole Compton-Gray LAST WORD An Advertising-Free Zone, Scott Moncrieffhttps://digitalcommons.andrews.edu/sm-108/1001/thumbnail.jp

The Student Movement Volume 108 Issue 6: Tayloring the Future: Andrews Inaugurates New President

HUMANS Filipino Pride and the Bayanihan Spirit, Savannah Tyler Intangible Impressions of Spiritual Life at Andrews, Savannah Tyler Meet the Majors: Part 2, Reagan McCain From Underdog to gRad-dog: A graduate student\u27s perspective on the transition from undergraduate to graduate school, Anna Rybachek ARTS & ENTERTAINMENT A New Chapter in Seasons, Nailea Soto A Report on the Eras Tour Movie, Nate Miller Gilmore Girls: The Downfall of College Rory, Audrey Lim How to Enter Music Circles on Campus, Reagan McCain NEWS Armenia - Azerbaijan Conflict, Katie Davis The Inauguration, Kiheon Chung Noche Latina: A Night to Celebrate Hispanic Heritage, Melissa Moore Understanding Tomorrow Today: The Fall 2023 Kingman Lecture, Jonathan Clough IDEAS My Struggle with Secular Music, Kiheon Chung No News Is Good News - But Here\u27s Some Good News!, Reagan Westerman Pakistan\u27s First Miss Universe Winner, Katie Davis PULSE American Melodies in Harmony with the AUSO, Aiko J. Ayala Rios Celebrating Filipino American History Month, Brooklyn Anderson Why We Can\u27t Seem to Get Enough Sleep, Alyssa Caruthers LAST WORD Do it For The Plot, Lily Burkehttps://digitalcommons.andrews.edu/sm-108/1005/thumbnail.jp

The structure of SSO2064, the first representative of Pfam family PF01796, reveals a novel two-domain zinc-ribbon OB-fold architecture with a potential acyl-CoA-binding role

The crystal structure of SSO2064, the first structural representative of Pfam family PF01796 (DUF35), reveals a two-domain architecture comprising an N-terminal zinc-ribbon domain and a C-terminal OB-fold domain. Analysis of the domain architecture, operon organization and bacterial orthologs combined with the structural features of SSO2064 suggests a role involving acyl-CoA binding for this family of proteins

Integrated genomic approaches implicate osteoglycin (Ogn) in the regulation of left ventricular mass

Left ventricular mass (LVM) and cardiac gene expression are complex traits regulated by factors both intrinsic and extrinsic to the heart. To dissect the major determinants of LVM, we combined expression quantitative trait locus1 and quantitative trait transcript (QTT) analyses of the cardiac transcriptome in the rat. Using these methods and in vitro functional assays, we identified osteoglycin (Ogn) as a major candidate regulator of rat LVM, with increased Ogn protein expression associated with elevated LVM. We also applied genome-wide QTT analysis to the human heart and observed that, out of 22,000 transcripts, OGN transcript abundance had the highest correlation with LVM. We further confirmed a role for Ogn in the in vivo regulation of LVM in Ogn knockout mice. Taken together, these data implicate Ogn as a key regulator of LVM in rats, mice and humans, and suggest that Ogn modifies the hypertrophic response to extrinsic factors such as hypertension and aortic stenosi

Aristolochene synthase structure and function

The 2.5Å structure of recombinant aristolochene synthase from Penicillium roqueforti reveals structural features common with other terpene cyclases. These features are critical to the cyclization of the substrate molecule farnesyl diphosphate into the product hydrocarbon aristolochene. In this mechanism, metal triggered carbocation formation initiates the reaction, which then proceeds through multiple, elaborate intermediate steps to yield one stereochemical isomer of aristolochene. The structure of aristolochene synthase in complex with the ligand farnesol provide a structural backdrop for this complex series of reactions. Despite minimal sequence identity, structural homology of this sesquiterpene cyclase with other terpene synthases suggests diversion from a common, primordial ancestor

Aristolochene synthase structure and function

The 2.5Å structure of recombinant aristolochene synthase from Penicillium roqueforti reveals structural features common with other terpene cyclases. These features are critical to the cyclization of the substrate molecule farnesyl diphosphate into the product hydrocarbon aristolochene. In this mechanism, metal triggered carbocation formation initiates the reaction, which then proceeds through multiple, elaborate intermediate steps to yield one stereochemical isomer of aristolochene. The structure of aristolochene synthase in complex with the ligand farnesol provide a structural backdrop for this complex series of reactions. Despite minimal sequence identity, structural homology of this sesquiterpene cyclase with other terpene synthases suggests diversion from a common, primordial ancestor

Structural basis of mechanochemical coupling in a hexameric molecular motor

The P4 protein of bacteriophage φ 12 is a hexameric molecular motor closely related to superfamily 4 helicases. P4 converts chemical energy from ATP hydrolysis into mechanical work, to translocate single-stranded RNA into a viral capsid. The molecular basis of mechanochemical coupling, i.e. how small ∼1 Å changes in the ATP-binding site are amplified into nanometer scale motion along the nucleic acid, is not understood at the atomic level. Here we study in atomic detail the mechanochemical coupling using structural and biochemical analyses of P4 mutants. We show that a conserved region, consisting of superfamily 4 helicase motifs H3 and H4 and loop L2, constitutes the moving lever of the motor. The lever tip encompasses an RNA-binding site that moves along the mechanical reaction coordinate. The lever is flanked by γ-phosphate sensors (Asn-234 and Ser-252) that report the nucleotide state of neighboring subunits and control the lever position. Insertion of an arginine finger (Arg-279) into the neighboring catalytic site is concomitant with lever movement and commences ATP hydrolysis. This ensures cooperative sequential hydrolysis that is tightly coupled to mechanical motion. Given the structural conservation, the mutated residues may play similar roles in other hexameric helicases and related molecular motors. © 2008 by The American Society for Biochemistry and Molecular Biology, Inc

Crystal structures and proposed structural/functional classification of three protozoan proteins from the isochorismatase superfamily

We have determined the crystal structures of three homologous proteins from the pathogenic protozoans Leishmania donovani, Leishmania major, and Trypanosoma cruzi. We propose that these proteins represent a new subfamily within the isochorismatase superfamily (CDD classification cd004310). Their overall fold and key active site residues are structurally homologous both to the biochemically well-characterized N-carbamoylsarcosine-amidohydrolase, a cysteine hydrolase, and to the phenazine biosynthesis protein PHZD (isochorismase), an aspartyl hydrolase. All three proteins are annotated as mitochondrial-associated ribonuclease Mar1, based on a previous characterization of the homologous protein from L. tarentolae. This would constitute a new enzymatic activity for this structural superfamily, but this is not strongly supported by the observed structures. In these protozoan proteins, the extended active site is formed by inter-subunit association within a tetramer, which implies a distinct evolutionary history and substrate specificity from the previously characterized members of the isochorismatase superfamily. The characterization of the active site is supported crystallographically by the presence of an unidentified ligand bound at the active site cysteine of the T. cruzi structure