2ge1: Difference between revisions
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{{Theoretical_model}} | {{Theoretical_model}} | ||
==PROTEIN COMPLEX OF A-STATE TYCC3-APO-PCP WITH THE PPTASE SFP (MODEL)== | |||
<StructureSection load='2ge1' size='340' side='right'caption='[[2ge1]]' 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=2GE1 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=2ge1 FirstGlance], [https://www.ebi.ac.uk/pdbsum/2ge1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ge1 ProSAT]</span></td></tr> | |||
-- | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Protein dynamics plays an important role in protein function. Many functionally important motions occur on the microsecond and low millisecond time scale and can be characterized by nuclear magnetic resonance relaxation experiments. We describe the different states of a peptidyl carrier protein (PCP) that play a crucial role in its function as a peptide shuttle in the nonribosomal peptide synthetases of the tyrocidine A system. Both apo-PCP (without the bound 4'-phosphopantetheine cofactor) and holo-PCP exist in two different stable conformations. We show that one of the apo conformations and one of the holo conformations are identical, whereas the two remaining conformations are only detectable by nuclear magnetic resonance spectroscopy in either the apo or holo form. We further demonstrate that this conformational diversity is an essential prerequisite for the directed movement of the 4'-PP cofactor and its interaction with externally acting proteins such as thioesterases and 4'-PP transferase. | |||
Conformational switches modulate protein interactions in peptide antibiotic synthetases.,Koglin A, Mofid MR, Lohr F, Schafer B, Rogov VV, Blum MM, Mittag T, Marahiel MA, Bernhard F, Dotsch V Science. 2006 Apr 14;312(5771):273-6. PMID:16614225<ref>PMID:16614225</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2ge1" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Theoretical Model]] | ||
[[Category: Large Structures]] | |||
== | |||
< | |||
[[Category: Bernhard, F]] | [[Category: Bernhard, F]] | ||
[[Category: Blum, M.-M]] | [[Category: Blum, M.-M]] | ||
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[[Category: Marahiel, M A]] | [[Category: Marahiel, M A]] | ||
[[Category: Rogov, V V]] | [[Category: Rogov, V V]] | ||
Latest revision as of 17:43, 29 December 2021
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PROTEIN COMPLEX OF A-STATE TYCC3-APO-PCP WITH THE PPTASE SFP (MODEL)PROTEIN COMPLEX OF A-STATE TYCC3-APO-PCP WITH THE PPTASE SFP (MODEL)
Structural highlights
Publication Abstract from PubMedProtein dynamics plays an important role in protein function. Many functionally important motions occur on the microsecond and low millisecond time scale and can be characterized by nuclear magnetic resonance relaxation experiments. We describe the different states of a peptidyl carrier protein (PCP) that play a crucial role in its function as a peptide shuttle in the nonribosomal peptide synthetases of the tyrocidine A system. Both apo-PCP (without the bound 4'-phosphopantetheine cofactor) and holo-PCP exist in two different stable conformations. We show that one of the apo conformations and one of the holo conformations are identical, whereas the two remaining conformations are only detectable by nuclear magnetic resonance spectroscopy in either the apo or holo form. We further demonstrate that this conformational diversity is an essential prerequisite for the directed movement of the 4'-PP cofactor and its interaction with externally acting proteins such as thioesterases and 4'-PP transferase. Conformational switches modulate protein interactions in peptide antibiotic synthetases.,Koglin A, Mofid MR, Lohr F, Schafer B, Rogov VV, Blum MM, Mittag T, Marahiel MA, Bernhard F, Dotsch V Science. 2006 Apr 14;312(5771):273-6. PMID:16614225[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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