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10.1016/j.bbapap.2015.12.006 http://scihub22266oqcxt.onion/10.1016/j.bbapap.2015.12.006 C4732270!4732270 !26708480     free     free     free Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 261.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 261.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 261.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 261.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 261.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 261.2 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\26708480 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Biochim+Biophys+Acta 2016 ; 1864 (3 ): 268-279 Nephropedia Template TP {{tp|p=26708480 |t=2016. Visualizing the tunnel in tryptophan synthase with crystallography: Insights into a selective filter for accommodating indole and rejecting water |pdf=|usr=}}{{26708480 }} gab.com Text Visualizing the tunnel in tryptophan synthase with crystallography: Insights into a selective filter for accommodating indole and rejecting water JO: Biochim Biophys Acta http://www.kidney.de/pget.php?&tw=1&pmid=26708480 #FOAvip Four new X-ray structures of tryptophan synthase (TS) crystallized with varying numbers of the amphipathic N-(4'-trifluoromethoxybenzoyl)-2-aminoethyl phosphate (F6) molecule are presented. These structures show one of the F6 ligands threaded into the tunnel from the ?-site and reveal a distinct hydrophobic region. Over this expanse, the interactions between F6 and the tunnel are primarily nonpolar, while the F6 phosphoryl group fits into a polar pocket of the ?-subunit active site. Further examination of TS structures reveals that one portion of the tunnel (T1) binds clusters of water molecules, whereas waters are not observed in the nonpolar F6 binding region of the tunnel (T2). MD simulation of another TS structure with an unobstructed tunnel also indicates the T2 region of the tunnel excludes water, consistent with a dewetted state that presents a significant barrier to the transfer of water into the closed ?-site. We conclude that hydrophobic molecules can freely diffuse between the ?- and ?-sites via the tunnel, while water does not. We propose that exclusion of water serves to inhibit reaction of water with the ?-aminoacrylate intermediate to form ammonium ion and pyruvate, a deleterious side reaction in the ??-catalytic cycle. Finally, while most TS structures show ?Phe280 partially blocking the tunnel between the ?- and ?-sites, new structures show an open tunnel, suggesting the flexibility of the ?Phe280 side chain. Flexible docking studies and MD simulations confirm that the dynamic behavior of ?Phe280 allows unhindered transfer of indole through the tunnel, therefore excluding a gating role for this residue. Twit Text FOAVip Visualizing the tunnel in tryptophan synthase with crystallography: Insights into a selective filter for accommodating indole and rejecting water ????Biochim Biophys Acta http://www.kidney.de/pget.php?&tw=1&pmid=26708480 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26708480 #FOAvip English Wikipedia <ref>{{Cite pmid|26708480 }}</ref> Visualizing the tunnel in tryptophan synthase with crystallography: Insights into a selective filter for accommodating indole and rejecting water #MMPMID26708480 Hilario E ; Caulkins BG ; Huang YM ; You W ; Chang CA ; Mueller LJ ; Dunn MF ; Fan L Biochim Biophys Acta 2016[Mar]; 1864 (3 ): 268-279 PMID26708480 show ga Four new X-ray structures of tryptophan synthase (TS) crystallized with varying numbers of the amphipathic N-(4'-trifluoromethoxybenzoyl)-2-aminoethyl phosphate (F6) molecule are presented. These structures show one of the F6 ligands threaded into the tunnel from the ?-site and reveal a distinct hydrophobic region. Over this expanse, the interactions between F6 and the tunnel are primarily nonpolar, while the F6 phosphoryl group fits into a polar pocket of the ?-subunit active site. Further examination of TS structures reveals that one portion of the tunnel (T1) binds clusters of water molecules, whereas waters are not observed in the nonpolar F6 binding region of the tunnel (T2). MD simulation of another TS structure with an unobstructed tunnel also indicates the T2 region of the tunnel excludes water, consistent with a dewetted state that presents a significant barrier to the transfer of water into the closed ?-site. We conclude that hydrophobic molecules can freely diffuse between the ?- and ?-sites via the tunnel, while water does not. We propose that exclusion of water serves to inhibit reaction of water with the ?-aminoacrylate intermediate to form ammonium ion and pyruvate, a deleterious side reaction in the ??-catalytic cycle. Finally, while most TS structures show ?Phe280 partially blocking the tunnel between the ?- and ?-sites, new structures show an open tunnel, suggesting the flexibility of the ?Phe280 side chain. Flexible docking studies and MD simulations confirm that the dynamic behavior of ?Phe280 allows unhindered transfer of indole through the tunnel, therefore excluding a gating role for this residue. |*Protein Conformation [MESH] |Binding Sites [MESH] |Catalysis [MESH] |Catalytic Domain [MESH] |Crystallography, X-Ray [MESH] |Hydrophobic and Hydrophilic Interactions [MESH] |Indoles/*chemistry [MESH] |Ligands [MESH] |Molecular Docking Simulation [MESH] |Molecular Dynamics Simulation [MESH] |Nanopores [MESH] |Salmonella typhimurium/enzymology [MESH] |Substrate Specificity [MESH] |Tryptophan Synthase/*chemistry [MESH]Visualizing the tunnel in tryptophan synthase with crystallography: In(epmc).pdf DeepDyve Pubget Overpricing