2gdw: Difference between revisions

Revision as of 19:26, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2gdw.png

Template:STRUCTURE 2gdw

Solution structure of the B. brevis TycC3-PCP in A/H-stateSolution structure of the B. brevis TycC3-PCP in A/H-state

Template:ABSTRACT PUBMED 16614225

About this StructureAbout this Structure

2GDW is a Single protein structure of sequence from Brevibacillus parabrevis. Full experimental information is available from OCA.

ReferenceReference

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

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Solution structure of the B. brevis TycC3-PCP in A/H-state'''
+===Solution structure of the B. brevis TycC3-PCP in A/H-state===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_16614225}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16614225 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16614225}}
 ==About this Structure==
-GDW is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Brevibacillus_parabrevis Brevibacillus parabrevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GDW OCA].
+GDW is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Brevibacillus_parabrevis Brevibacillus parabrevis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GDW OCA].
 ==Reference==
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 [[Category: Rogov, V V.]]
 [[Category: Three-helix bundle]]
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