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Instruments / Technical Area	Publication Details	Published
I24-Microfocus Macromolecular Crystallography	The N-terminal acetylation of Sir3 stabilizes its binding to the nucleosome core particle Nadia Arnaudo , Israel S. Fernandez , Stephen H. Mclaughlin , Sew Y. Peak-Chew , Daniela Rhodes , Fabrizio Martino Nature Structural & Molecular Biology DOI: 10.1038/nsmb.2641 PMID: 23934150 Show Abstract ▼ Abstract: The N-terminal acetylation of Sir3 is essential for heterochromatin establishment and maintenance in yeast, but its mechanism of action is unknown. The crystal structure of the N-terminally acetylated BAH domain of Saccharomyces cerevisiae Sir3 bound to the nucleosome core particle reveals that the N-terminal acetylation stabilizes the interaction of Sir3 with the nucleosome. Additionally, we present a new method for the production of proteinnucleosome complexes for structural analysis.	Aug 2013
I04-Macromolecular Crystallography	Unusual base pairing during the decoding of a stop codon by the ribosome Israel S. Fernandez , Chyan Leong Ng , Ann C. Kelley , Guowei Wu , Yi-Tao Yu , Venki Ramakrishnan Nature 500 (7460), 107 - 110 DOI: 10.1038/nature12302 PMID: 23812587 Show Abstract ▼ Abstract: During normal translation, the binding of a release factor to one of the three stop codons (UGA, UAA or UAG) results in the termination of protein synthesis. However, modification of the initial uridine to a pseudouridine (Ψ) allows efficient recognition and read-through of these stop codons by a transfer RNA (tRNA), although it requires the formation of two normally forbidden purine–purine base pairs1. Here we determined the crystal structure at 3.1 Å resolution of the 30S ribosomal subunit in complex with the anticodon stem loop of tRNASer bound to the ΨAG stop codon in the A site. The ΨA base pair at the first position is accompanied by the formation of purine–purine base pairs at the second and third positions of the codon, which show an unusual Watson–Crick/Hoogsteen geometry. The structure shows a previously unsuspected ability of the ribosomal decoding centre to accommodate non-canonical base pairs.	Jun 2013
I04-Macromolecular Crystallography	Elongation factor G bound to the ribosome in an intermediate state of translocation David S. Tourigny , Israel S. Fernandez , Ann C. Kelley , Venki Ramakrishnan Science 340 (6140), 1235490 - 1235490 DOI: 10.1126/science.1235490 PMID: 23812720 Show Abstract ▼ Abstract: A key step of translation by the ribosome is translocation, which involves the movement of messenger RNA (mRNA) and transfer RNA (tRNA) with respect to the ribosome. This allows a new round of protein chain elongation by placing the next mRNA codon in the A site of the 30S subunit. Translocation proceeds through an intermediate state in which the acceptor ends of the tRNAs have moved with respect to the 50S subunit but not the 30S subunit, to form hybrid states. The guanosine triphosphatase (GTPase) elongation factor G (EF-G) catalyzes the subsequent movement of mRNA and tRNA with respect to the 30S subunit. Here, we present a crystal structure at 3 angstrom resolution of the Thermus thermophilus ribosome with a tRNA in the hybrid P/E state bound to EF-G with a GTP analog. The structure provides insights into structural changes that facilitate translocation and suggests a common GTPase mechanism for EF-G and elongation factor Tu.	Jun 2013
I04-Macromolecular Crystallography	Crystal structure of a bioactive pactamycin analog bound to the 30S ribosomal subunit David S. Tourigny , Israel S. Fernandez , Ann C. Kelley , Ramkrishna Reddy Vakiti , Amit Kumar Chattopadhyay , Stéphane Dorich , Stephen Hanessian , Venki Ramakrishnan Journal Of Molecular Biology DOI: 10.1016/j.jmb.2013.05.004 PMID: 23702293 Open Access Show Abstract ▼ Abstract: Biosynthetically and chemically derived analogs of the antibiotic pactamycin and de-6-methylsalicylyl (MSA)-pactamycin have attracted recent interest as potential antiprotozoal and antitumor drugs. Here, we report a 3.1-Å crystal structure of de-6-MSA-pactamycin bound to its target site on the Thermus thermophilus 30S ribosomal subunit. Although de-6-MSA-pactamycin lacks the MSA moiety, it shares the same binding site as pactamycin and induces a displacement of nucleic acid template bound at the E-site of the 30S. The structure highlights unique interactions between this pactamycin analog and the ribosome, which paves the way for therapeutic development of related compounds.	May 2013

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