1e11: Difference between revisions
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{{Theoretical_model}} | |||
==MODEL STRUCTURE OF ELECTRON TRANSFERRING FLAVOPROTEIN FROM METHYLOPHILUS METHYLOTROPUS (C-ALPHA ONLY)== | |||
<StructureSection load='1e11' size='340' side='right'caption='[[1e11]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E11 FirstGlance]. <br> | |||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1e11 FirstGlance], [https://www.ebi.ac.uk/pdbsum/1e11 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e11 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Small angle x-ray solution scattering has been used to generate a low resolution, model-independent molecular envelope structure for electron-transferring flavoprotein (ETF) from Methylophilus methylotrophus (sp. W(3)A(1)). Analysis of both the oxidized and 1-electron-reduced (anionic flavin semiquinone) forms of the protein revealed that the solution structures of the protein are similar in both oxidation states. Comparison of the molecular envelope of ETF from the x-ray scattering data with previously determined structural models of the protein suggests that ETF samples a range of conformations in solution. These conformations correspond to a rotation of domain II with respect to domains I and III about two flexible "hinge" sequences that are unique to M. methylotrophus ETF. The x-ray scattering data are consistent with previous models concerning the interaction of M. methylotrophus ETF with its physiological redox partner, trimethylamine dehydrogenase. Our data reveal that an "induced fit" mechanism accounts for the assembly of the trimethylamine dehydrogenase-ETF electron transfer complex, consistent with spectroscopic and modeling studies of the assembly process. | |||
X-ray scattering studies of Methylophilus methylotrophus (sp. W3A1) electron-transferring flavoprotein. Evidence for multiple conformational states and an induced fit mechanism for assembly with trimethylamine dehydrogenase.,Jones M, Basran J, Sutcliffe MJ, Gunter Grossmann J, Scrutton NS J Biol Chem. 2000 Jul 14;275(28):21349-54. PMID:10766748<ref>PMID:10766748</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1e11" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Theoretical Model]] | |||
[[Category: Large Structures]] | |||
[[Category: Chohan, K K]] | |||
[[Category: Scrutton, N S]] | |||
[[Category: Sutcliffe, M J]] | |||
Latest revision as of 12:33, 21 July 2021
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MODEL STRUCTURE OF ELECTRON TRANSFERRING FLAVOPROTEIN FROM METHYLOPHILUS METHYLOTROPUS (C-ALPHA ONLY)MODEL STRUCTURE OF ELECTRON TRANSFERRING FLAVOPROTEIN FROM METHYLOPHILUS METHYLOTROPUS (C-ALPHA ONLY)
Structural highlights
Publication Abstract from PubMedSmall angle x-ray solution scattering has been used to generate a low resolution, model-independent molecular envelope structure for electron-transferring flavoprotein (ETF) from Methylophilus methylotrophus (sp. W(3)A(1)). Analysis of both the oxidized and 1-electron-reduced (anionic flavin semiquinone) forms of the protein revealed that the solution structures of the protein are similar in both oxidation states. Comparison of the molecular envelope of ETF from the x-ray scattering data with previously determined structural models of the protein suggests that ETF samples a range of conformations in solution. These conformations correspond to a rotation of domain II with respect to domains I and III about two flexible "hinge" sequences that are unique to M. methylotrophus ETF. The x-ray scattering data are consistent with previous models concerning the interaction of M. methylotrophus ETF with its physiological redox partner, trimethylamine dehydrogenase. Our data reveal that an "induced fit" mechanism accounts for the assembly of the trimethylamine dehydrogenase-ETF electron transfer complex, consistent with spectroscopic and modeling studies of the assembly process. X-ray scattering studies of Methylophilus methylotrophus (sp. W3A1) electron-transferring flavoprotein. Evidence for multiple conformational states and an induced fit mechanism for assembly with trimethylamine dehydrogenase.,Jones M, Basran J, Sutcliffe MJ, Gunter Grossmann J, Scrutton NS J Biol Chem. 2000 Jul 14;275(28):21349-54. PMID:10766748[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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