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Instruments / Technical Area	Publication Details	Published	Actions
Krios II-Titan Krios II at Diamond	Cryo-electron microscopy reveals two distinct type IV pili assembled by the same bacterium Alexander Neuhaus , Muniyandi Selvaraj , Ralf Salzer , Julian D. Langer , Kerstin Kruse , Lennart Kirchner , Kelly Sanders , Bertram Daum , Beate Averhoff , Vicki A. M. Gold Nature Communications 11 DOI: 10.1038/s41467-020-15650-w Diamond Proposal Number(s): [18258] Open Access Show Abstract ▼ Abstract: Type IV pili are flexible filaments on the surface of bacteria, consisting of a helical assembly of pilin proteins. They are involved in bacterial motility (twitching), surface adhesion, biofilm formation and DNA uptake (natural transformation). Here, we use cryo-electron microscopy and mass spectrometry to show that the bacterium Thermus thermophilus produces two forms of type IV pilus (‘wide’ and ‘narrow’), differing in structure and protein composition. Wide pili are composed of the major pilin PilA4, while narrow pili are composed of a so-far uncharacterized pilin which we name PilA5. Functional experiments indicate that PilA4 is required for natural transformation, while PilA5 is important for twitching motility.	May 2020
I02-Macromolecular Crystallography	The structure of the human respiratory syncytial virus M2-1 protein bound to the interaction domain of the phosphoprotein P defines the orientation of the complex Muniyandi Selvaraj , Kavestri Yegambaram , Eleanor J. A. A. Todd , Charles-adrien Richard , Rachel L. Dods , Georgia M. Pangratiou , Chi H. Trinh , Sophie L. Moul , James C. Murphy , Jamel Mankouri , Jean-françois Éléouët , John N. Barr , Thomas A. Edwards Mbio 9 DOI: 10.1128/mBio.01554-18 Diamond Proposal Number(s): [10305] Open Access Show Abstract ▼ Abstract: Human respiratory syncytial virus (HRSV) is a negative-stranded RNA virus that causes a globally prevalent respiratory infection, which can cause life-threatening illness, particularly in the young, elderly, and immunocompromised. HRSV multiplication depends on replication and transcription of the HRSV genes by the virus-encoded RNA-dependent RNA polymerase (RdRp). For replication, this complex comprises the phosphoprotein (P) and the large protein (L), whereas for transcription, the M2-1 protein is also required. M2-1 is recruited to the RdRp by interaction with P and also interacts with RNA at overlapping binding sites on the M2-1 surface, such that binding of these partners is mutually exclusive. The molecular basis for the transcriptional requirement of M2-1 is unclear, as is the consequence of competition between P and RNA for M2-1 binding, which is likely a critical step in the transcription mechanism. Here, we report the crystal structure at 2.4 Å of M2-1 bound to the P interaction domain, which comprises P residues 90 to 110. The P90–110 peptide is alpha helical, and its position on the surface of M2-1 defines the orientation of the three transcriptase components within the complex. The M2-1/P interface includes ionic, hydrophobic, and hydrogen bond interactions, and the critical contribution of these contacts to complex formation was assessed using a minigenome assay. The affinity of M2-1 for RNA and P ligands was quantified using fluorescence anisotropy, which showed high-affinity RNAs could outcompete P. This has important implications for the mechanism of transcription, particularly the events surrounding transcription termination and synthesis of poly(A) sequences.	Nov 2018

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