2gdw

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|ACTIVITY=
|ACTIVITY=
|GENE= tycC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=54914 Brevibacillus parabrevis])
|GENE= tycC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=54914 Brevibacillus parabrevis])
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|DOMAIN=
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|RELATEDENTRY=[[2gdx|2GDX]], [[2gdy|2GDY]], [[2ge1|2GE1]], [[2ge0|2GE0]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2gdw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gdw OCA], [http://www.ebi.ac.uk/pdbsum/2gdw PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2gdw RCSB]</span>
}}
}}
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[[Category: three-helix bundle]]
[[Category: three-helix bundle]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:03:32 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:15:21 2008''

Revision as of 00:15, 31 March 2008


PDB ID 2gdw

Drag the structure with the mouse to rotate
Gene: tycC (Brevibacillus parabrevis)
Related: 2GDX, 2GDY, 2GE1, 2GE0


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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.

About this Structure

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

Reference

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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