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< | ==Solution structure of the B. brevis TycC3-PCP in H-state== | ||
<StructureSection load='2gdx' size='340' side='right'caption='[[2gdx]]' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2gdx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Brevibacillus_parabrevis Brevibacillus parabrevis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GDX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GDX FirstGlance]. <br> | |||
or | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2gdx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gdx OCA], [https://pdbe.org/2gdx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gdx RCSB], [https://www.ebi.ac.uk/pdbsum/2gdx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gdx ProSAT]</span></td></tr> | ||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/TYCC_BREPA TYCC_BREPA] Incorporates six amino acids (for tyrocidine A, Asn, Gln, Tyr, Val, Orn, and Leu) in their L-configuration into the peptide product. | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gd/2gdx_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2gdx ConSurf]. | |||
<div style="clear:both"></div> | |||
<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 2gdx" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
== | |||
[[Category: Brevibacillus parabrevis]] | [[Category: Brevibacillus parabrevis]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Bernhard | [[Category: Bernhard F]] | ||
[[Category: Doetsch | [[Category: Doetsch V]] | ||
[[Category: Koglin | [[Category: Koglin A]] | ||
[[Category: Loehr | [[Category: Loehr F]] | ||
[[Category: Marahiel | [[Category: Marahiel MA]] | ||
[[Category: Rogov | [[Category: Rogov VV]] | ||
Latest revision as of 21:58, 29 May 2024
Solution structure of the B. brevis TycC3-PCP in H-stateSolution structure of the B. brevis TycC3-PCP in H-state
Structural highlights
FunctionTYCC_BREPA Incorporates six amino acids (for tyrocidine A, Asn, Gln, Tyr, Val, Orn, and Leu) in their L-configuration into the peptide product. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. 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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