{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,29]],"date-time":"2026-10-29T10:38:13Z","timestamp":1793270293061,"version":"4.5.0"},"reference-count":42,"publisher":"National Academy of Sciences","issue":"28","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2009,7,14]]},"abstract":"<jats:p>The negative-strand RNA viruses (NSRVs) are unique because their nucleocapsid, not the naked RNA, is the active template for transcription and replication. The viral polymerase of nonsegmented NSRVs contains a large polymerase catalytic subunit (L) and a nonenzymatic cofactor, the phosphoprotein (P). Insight into how P delivers the polymerase complex to the nucleocapsid has long been pursued by reverse genetics and biochemical approaches. Here, we present the X-ray crystal structure of the C-terminal domain of P of vesicular stomatitis virus, a prototypic nonsegmented NSRV, bound to nucleocapsid-like particles. P binds primarily to the C-terminal lobe of 2 adjacent N proteins within the nucleocapsid. This binding mode is exclusive to the nucleocapsid, not the nucleocapsid (N) protein in other existing forms. Localization of phosphorylation sites within P and their proximity to the RNA cavity give insight into how the L protein might be oriented to access the RNA template.<\/jats:p>","DOI":"10.1073\/pnas.0903228106","type":"journal-article","created":{"date-parts":[[2009,7,1]],"date-time":"2009-07-01T21:40:50Z","timestamp":1246484450000},"page":"11713-11718","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":127,"title":["Structure of the vesicular stomatitis virus nucleocapsid in complex with the nucleocapsid-binding domain of the small polymerase cofactor, P"],"prefix":"10.1073","volume":"106","author":[{"given":"Todd J.","family":"Green","sequence":"first","affiliation":[{"name":"Department of Microbiology, University of Alabama School of Medicine, 1025 18th Street South, Birmingham, AL 35294"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ming","family":"Luo","sequence":"additional","affiliation":[{"name":"Department of Microbiology, University of Alabama School of Medicine, 1025 18th Street South, Birmingham, AL 35294"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2009,7,14]]},"reference":[{"key":"e_1_3_3_1_2","doi-asserted-by":"publisher","DOI":"10.1016\/0022-2836(66)90143-4"},{"key":"e_1_3_3_2_2","doi-asserted-by":"publisher","DOI":"10.1128\/jvi.10.2.297-309.1972"},{"key":"e_1_3_3_3_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(17)33297-0"},{"key":"e_1_3_3_4_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.1126953"},{"key":"e_1_3_3_5_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.1125280"},{"key":"e_1_3_3_6_2","doi-asserted-by":"publisher","DOI":"10.1128\/JVI.00935-07"},{"key":"e_1_3_3_7_2","doi-asserted-by":"publisher","DOI":"10.1016\/0168-1702(87)90023-2"},{"key":"e_1_3_3_8_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1348-0421.2005.tb03666.x"},{"key":"e_1_3_3_9_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.89.14.6570"},{"key":"e_1_3_3_10_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.270.41.24100"},{"key":"e_1_3_3_11_2","doi-asserted-by":"publisher","DOI":"10.1002\/j.1460-2075.1995.tb07107.x"},{"key":"e_1_3_3_12_2","doi-asserted-by":"publisher","DOI":"10.1128\/jvi.66.10.5842-5848.1992"},{"key":"e_1_3_3_13_2","doi-asserted-by":"publisher","DOI":"10.1006\/viro.1996.8401"},{"key":"e_1_3_3_14_2","doi-asserted-by":"publisher","DOI":"10.1128\/jvi.71.11.8167-8175.1997"},{"key":"e_1_3_3_15_2","doi-asserted-by":"publisher","DOI":"10.1128\/JVI.80.6.2808-2814.2006"},{"key":"e_1_3_3_16_2","doi-asserted-by":"publisher","DOI":"10.1128\/JVI.79.13.8101-8112.2005"},{"key":"e_1_3_3_17_2","doi-asserted-by":"publisher","DOI":"10.1128\/jvi.69.12.7718-7723.1995"},{"key":"e_1_3_3_18_2","doi-asserted-by":"publisher","DOI":"10.1128\/JVI.74.20.9515-9524.2000"},{"key":"e_1_3_3_19_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.83.23.8873"},{"key":"e_1_3_3_20_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.90.21.10375"},{"key":"e_1_3_3_21_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.84.16.5655"},{"key":"e_1_3_3_22_2","doi-asserted-by":"publisher","DOI":"10.1006\/viro.1997.8823"},{"key":"e_1_3_3_23_2","doi-asserted-by":"publisher","DOI":"10.1016\/0042-6822(88)90505-3"},{"key":"e_1_3_3_24_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.jmb.2008.07.028"},{"key":"e_1_3_3_25_2","doi-asserted-by":"publisher","DOI":"10.1128\/jvi.62.8.2658-2664.1988"},{"key":"e_1_3_3_26_2","doi-asserted-by":"publisher","DOI":"10.1128\/jvi.62.8.2799-2807.1988"},{"key":"e_1_3_3_27_2","doi-asserted-by":"publisher","DOI":"10.1016\/0042-6822(88)90477-1"},{"key":"e_1_3_3_28_2","doi-asserted-by":"publisher","DOI":"10.1128\/jvi.15.6.1348-1356.1975"},{"key":"e_1_3_3_29_2","doi-asserted-by":"publisher","DOI":"10.1128\/JVI.77.1.732-738.2003"},{"key":"e_1_3_3_30_2","doi-asserted-by":"publisher","DOI":"10.1107\/S0907444998003254"},{"key":"e_1_3_3_31_2","doi-asserted-by":"publisher","DOI":"10.1128\/JVI.01035-06"},{"key":"e_1_3_3_32_2","volume-title":"Preparation and Analysis of Protein Crystals","author":"Mcpherson A","year":"1982","unstructured":"A Mcpherson Preparation and Analysis of Protein Crystals (John Wiley, New York, 1982)."},{"key":"e_1_3_3_33_2","first-page":"307","volume-title":"Methods in Enzymology","author":"Otwinowski Z","year":"1997","unstructured":"Z Otwinowski, W Minor, Processsing of x-ray diffraction data collected in oscillation mode. 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