2fwl: Difference between revisions

Revision as of 07:25, 29 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:2fwl.png

Template:STRUCTURE 2fwl

The cytochrome c552/CuA complex from Thermus thermophilusThe cytochrome c552/CuA complex from Thermus thermophilus

Template:ABSTRACT PUBMED 16554303

About this StructureAbout this Structure

2FWL is a Protein complex structure of sequences from Thermus thermophilus. Full experimental information is available from OCA.

ReferenceReference

The electron transfer complex between cytochrome c552 and the CuA domain of the Thermus thermophilus ba3 oxidase. A combined NMR and computational approach., Muresanu L, Pristovsek P, Lohr F, Maneg O, Mukrasch MD, Ruterjans H, Ludwig B, Lucke C, J Biol Chem. 2006 May 19;281(20):14503-13. Epub 2006 Mar 22. PMID:16554303

Page seeded by OCA on Tue Jul 29 07:25:06 2008

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

OCA

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-'''The cytochrome c552/CuA complex from Thermus thermophilus'''
+===The cytochrome c552/CuA complex from Thermus thermophilus===
-==Overview==
+<!--
-The structural analysis of the redox complex between the soluble cytochrome c552 and the membrane-integral cytochrome ba3 oxidase of Thermus thermophilus is complicated by the transient nature of this protein-protein interaction. Using NMR-based chemical shift perturbation mapping, however, we identified the contact regions between cytochrome c552 and the CuA domain, the fully functional water-soluble fragment of subunit II of the ba3 oxidase. First we determined the complete backbone resonance assignments of both proteins for each redox state. Subsequently, two-dimensional [15N,1H]TROSY spectra recorded for each redox partner both in free and complexed state indicated those surface residues affected by complex formation between the two proteins. This chemical shift analysis performed for both redox states provided a topological description of the contact surface on each partner molecule. Remarkably, very pronounced indirect effects, which were observed on the back side of the heme cleft only in the reduced state, suggested that alterations of the electron distribution in the porphyrin ring due to formation of the protein-protein complex are apparently sensed even beyond the heme propionate groups. The contact residues of each redox partner, as derived from the chemical shift perturbation mapping, were employed for a protein-protein docking calculation that provided a structure ensemble of 10 closely related conformers representing the complex between cytochrome c552 and the CuA domain. Based on these structures, the electron transfer pathway from the heme of cytochrome c552 to the CuA center of the ba3 oxidase has been predicted.
+The line below this paragraph, {{ABSTRACT_PUBMED_16554303}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16554303 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16554303}}
 ==About this Structure==
-FWL is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FWL OCA].
+FWL is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FWL OCA].
 ==Reference==
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 [[Category: Electron transfer pathway]]
 [[Category: Redox protein complex]]
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