AB, E.

Robillard, G.T.

Scheek, R.M.

English

Proceedings - University of Groningen

   University of GroningenSolution Structure of E. coli IIBcellobiose of the PEP-dependent PTSAB, E.; Scheek, R.M.; Robillard, G.T.IMPORTANT NOTE: You are advised to consult the publisher's version (publisher's PDF) if you wish to cite fromit. Please check the document version below.Document VersionPublisher's PDF, also known as Version of recordPublication date:1996Link to publication in University of Groningen/UMCG research databaseCitation for published version (APA):AB, E., Scheek, R. M., & Robillard, G. T. (1996). Solution Structure of E. coli IIBcellobiose of the PEP-dependent PTS.CopyrightOther than for strictly personal use, it is not permitted to download or to forward/distribute the text or part of it without the consent of theauthor(s) and/or copyright holder(s), unless the work is under an open content license (like Creative Commons).The publication may also be distributed here under the terms of Article 25fa of the Dutch Copyright Act, indicated by the “Taverne” license.More information can be found on the University of Groningen website: https://www.rug.nl/library/open-access/self-archiving-pure/taverne-amendment.Take-down policyIf you believe that this document breaches copyright please contact us providing details, and we will remove access to the work immediatelyand investigate your claim.Downloaded from the University of Groningen/UMCG research database (Pure): http://www.rug.nl/research/portal. For technical reasons thenumber of authors shown on this cover page is limited to 10 maximum.Download date: 04-06-2022Al 3D structures: experimental determination P-Al-05 3D RECONSTRUCTION OF BOVINE PAPILLOMAVIRUS VISUALIZED AT 9A B.L. TRUS”‘. H.L. GREENSTONE” R.B.S. RODEN” J.T. SCHILLER*AND F.P. BGGY3 ’ DCRT-CBEL; ’ NCI-LCO; 3 NIAMS-LSB; NM, Bethesda, MD 20892, USA Purpose: We have been using bovine papillomavirus (BPV) to extend the resolution of 3D density maps reconstructed from cryo-microgmphs with a view to visuahsing protein domains and ultimately tertiary structure.BPV has a diameter of - 600 A. a T number of 7, and two shell proteins (Ll and L2) in a ratio of 30 : 1 (I). Methods: Micrographs were recorded on a Philips EM4OORT using a modified Gatan cooling holder, digitized on a Perkin Elmer IOIOMG, pnproccssed and reconstructed as described (2). Origin and orientational refinement ensued to high precision (3). Results: Resolution of the 3D reconstruction from -200 images was assessed by FRC ccefflcents (4) using the 2- sigma curve as the threshold for meaningful signal and a new method based on the spectral signal-to-noise ratio (5). Two independent reconstructions compared well by FRC (6) and DPR (7). Conclusions: The 3D reconstruction was statistically significant to 9A resolution by all criteria applied. Features are seen in greater detail at increasing resolution. The button of density at the center of the 5-fold pentons may mark the location of the minor capsid protein L2. References: (1) Baker et al. (1991) Biophys. J. 60 : 1445 (2) Newcomb et al. (1993) J. Mol. Biol. 232 : 499-51 I. (3) Baker and Cheng (1996) J.Struct. Biol. 116: 120-130. (4) Conway et al. (1993) Strut. Biol. 111: 222-233. (5) Unser et al. (1996) manuscript in submission. (6) Saxtonand Baumeister (1982) J. Microscopy 127 : 7 (7) Frank et al. (1981) Science 214 : 1353 P-Al-07 SOLUTION CONFORMATION OF [PRO 7,131] aA-CONOT$XIN PIV+ KIM S-M, I-WANG K-J, KIM S-K , SHON K- J,z GRAY m3 OLIVE%4 BM,’ RMBR J, f-IAN K-H.’ Biomoleculnr Stntc$e +U.. ZB sff O&‘mk$z ~~$&),%$?%%&y, Univ. of utbh (USA), ClaytonLab. for eptide Biology, Salk Inat.(LJgA) Purpose:Anapproaehtothestudyofli qnd- recpetor interactrons is to investifiate the b - resolution structures of varjous.lqa& which are molecules of less cornplexr~ than the receptor, while systematieaIl~ coIktmg relevant information regarding ligand-receptor interactions. Methods: NMR experiments were performed in a phase-sensitive mode using a Vanan UNITY 500 spectrometer at 14°C and 25°C. Calculation of structures were done us’ and back-calculation of NO T&Y distance-geometry 324 NOE restraints. spectrum using Results : The final set of the 12 @at stn&ures had an average backbone mtisg0%0.9SA and back ealculqtion of 8 spectrum had R&57. rided 4~ewNOEreatmints and ‘elded e,R-factors ofR,=O.641 and Conclupions: The solution structure of [Pro 7,133 aA-conotoxln P,, should provide a framework fbr &rue&a atrudka for the entire uA family of Conotoxma &n&&t&ii for acetylcholine receptor-targeted eonoto&ts. P-Al-06 SECONDARY STRUCTURE OF HUMAN SEMINAL PLASMA PROSTATIC INHIBIN: BIOPHYSICAL STUDY RASTOGI VK, CHARY KVR, GOVIL G. Tata Institute of Fundamental Research, Mumbai. (IN) Purpose: Prostatic Inhibin (HSPI) protein (M, = 10.4 kDa) has been isolated from human seminal plasma to study the three-dimensional structure. Methods: CD, fluorescence and 2D NMR experiments have been carried out in aqueous solution at different pH and temperature. Results & Conclusions: CD measurements revealed that HSPI has a rigid and ordered structure. Fluorescence studies showed that both the tryptophans in the protein are in hydrophobic core. Analysis of NMR spectra has enabled us to identify and assign nearly all spin systems, NMR studies revealed that the protein predominantly adopts anti-parallel P-sheet conformation. No o-helical segments are present. The segments C42-Y43-E44-T45 and SWV89-S90-E91 are found to adopt type II p- turns. P-Al-08 t-hWitmSlOnretrveafE.cstim- of the lpz”s Af3 E, RCWLLARR GT. GBWBIOSON, Vaiverslty of Qoaippsa,0reai@= @‘W molecular dynainics calculations were performed in to &ain a clursct of a-m. In order to sh5piifytb3assinnmqgtof~~~es,we tiwiedsd\flringbMD .20QONOBWnaitiesa 28 

Solution Structure of E. coli IIBcellobiose of the PEP-dependent PTS

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Solution Structure of E. coli IIBcellobiose of the PEP-dependent PTS

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