Use my Search Websuite to scan PubMed, PMCentral, Journal Hosts and Journal Archives, FullText. Kick-your-searchterm to multiple Engines kick-your-query now !>

A dictionary by aggregated review articles of nephrology, medicine and the life sciences Your one-stop-run pathway from word to the immediate pdf of peer-reviewed on-topic knowledge.

10.1073/pnas.1707102114 http://scihub22266oqcxt.onion/10.1073/pnas.1707102114 C5676892!5676892 !29078304     free     free     free Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 251.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 251.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 251.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 251.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 251.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\29078304 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Proc+Natl+Acad+Sci+U+S+A 2017 ; 114 (44 ): 11697-11702 Nephropedia Template TP {{tp|p=29078304 |t=2017. Structures of Q? virions, virus-like particles, and the Q?-MurA complex reveal internal coat proteins and the mechanism of host lysis |pdf=|usr=}}{{29078304 }} gab.com Text Structures of Q virions, virus-like particles, and the Q -MurA complex reveal internal coat proteins and the mechanism of host lysis JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=29078304 #FOAvip In single-stranded RNA bacteriophages (ssRNA phages) a single copy of the maturation protein binds the genomic RNA (gRNA) and is required for attachment of the phage to the host pilus. For the canonical Allolevivirus Q? the maturation protein, A(2), has an additional role as the lysis protein, by its ability to bind and inhibit MurA, which is involved in peptidoglycan biosynthesis. Here, we determined structures of Q? virions, virus-like particles, and the Q?-MurA complex using single-particle cryoelectron microscopy, at 4.7-Å, 3.3-Å, and 6.1-Å resolutions, respectively. We identified the outer surface of the ?-region in A(2) as the MurA-binding interface. Moreover, the pattern of MurA mutations that block Q? lysis and the conformational changes of MurA that facilitate A(2) binding were found to be due to the intimate fit between A(2) and the region encompassing the closed catalytic cleft of substrate-liganded MurA. Additionally, by comparing the Q? virion with Q? virus-like particles that lack a maturation protein, we observed a structural rearrangement in the capsid coat proteins that is required to package the viral gRNA in its dominant conformation. Unexpectedly, we found a coat protein dimer sequestered in the interior of the virion. This coat protein dimer binds to the gRNA and interacts with the buried ?-region of A(2), suggesting that it is sequestered during the early stage of capsid formation to promote the gRNA condensation required for genome packaging. These internalized coat proteins are the most asymmetrically arranged major capsid proteins yet observed in virus structures. Twit Text FOAVip Structures of Q virions, virus-like particles, and the Q -MurA complex reveal internal coat proteins and the mechanism of host lysis ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=29078304 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29078304 #FOAvip English Wikipedia <ref>{{Cite pmid|29078304 }}</ref> Structures of Q? virions, virus-like particles, and the Q?-MurA complex reveal internal coat proteins and the mechanism of host lysis #MMPMID29078304 Cui Z ; Gorzelnik KV ; Chang JY ; Langlais C ; Jakana J ; Young R ; Zhang J Proc Natl Acad Sci U S A 2017[Oct]; 114 (44 ): 11697-11702 PMID29078304 show ga In single-stranded RNA bacteriophages (ssRNA phages) a single copy of the maturation protein binds the genomic RNA (gRNA) and is required for attachment of the phage to the host pilus. For the canonical Allolevivirus Q? the maturation protein, A(2), has an additional role as the lysis protein, by its ability to bind and inhibit MurA, which is involved in peptidoglycan biosynthesis. Here, we determined structures of Q? virions, virus-like particles, and the Q?-MurA complex using single-particle cryoelectron microscopy, at 4.7-Å, 3.3-Å, and 6.1-Å resolutions, respectively. We identified the outer surface of the ?-region in A(2) as the MurA-binding interface. Moreover, the pattern of MurA mutations that block Q? lysis and the conformational changes of MurA that facilitate A(2) binding were found to be due to the intimate fit between A(2) and the region encompassing the closed catalytic cleft of substrate-liganded MurA. Additionally, by comparing the Q? virion with Q? virus-like particles that lack a maturation protein, we observed a structural rearrangement in the capsid coat proteins that is required to package the viral gRNA in its dominant conformation. Unexpectedly, we found a coat protein dimer sequestered in the interior of the virion. This coat protein dimer binds to the gRNA and interacts with the buried ?-region of A(2), suggesting that it is sequestered during the early stage of capsid formation to promote the gRNA condensation required for genome packaging. These internalized coat proteins are the most asymmetrically arranged major capsid proteins yet observed in virus structures. |Alkyl and Aryl Transferases/chemistry/genetics/*metabolism [MESH] |Allolevivirus/*ultrastructure [MESH] |Capsid Proteins/chemistry [MESH] |Capsid/chemistry [MESH] |Gene Expression Regulation, Viral [MESH] |Protein Conformation [MESH] |RNA, Viral [MESH]Structures of Q? virions, virus-like particles, and the Q?-MurA comple(epmc).pdf DeepDyve Pubget Overpricing