2b1k: Difference between revisions

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[[Image:2b1k.jpg|left|200px]]
[[Image:2b1k.jpg|left|200px]]


{{Structure
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|GENE= ccmg ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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|DOMAIN=
{{STRUCTURE_2b1k| PDB=2b1k |  SCENE= }}  
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2b1k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b1k OCA], [http://www.ebi.ac.uk/pdbsum/2b1k PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2b1k RCSB]</span>
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'''Crystal structure of E. coli CcmG protein'''
'''Crystal structure of E. coli CcmG protein'''
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[[Category: Ouyang, N.]]
[[Category: Ouyang, N.]]
[[Category: Xia, Z X.]]
[[Category: Xia, Z X.]]
[[Category: c-terminal thioredoxin-like domain]]
[[Category: C-terminal thioredoxin-like domain]]
[[Category: fingerprint rigion]]
[[Category: Fingerprint rigion]]
[[Category: n-terminal beta-sheet]]
[[Category: N-terminal beta-sheet]]
 
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Revision as of 19:44, 3 May 2008

File:2b1k.jpg

Template:STRUCTURE 2b1k

Crystal structure of E. coli CcmG protein


OverviewOverview

CcmG, also designated DsbE, functions as a periplasmic protein thiol:disulfide oxidoreductase and is required for cytochrome c maturation. Here we report the crystal structures of Escherichia coli CcmG and its two mutants, P144A and the N-terminal fifty seven-residue deletion mutant, and two additional deletion mutants were studied by circular dichroism. Structural comparison of E. coli CcmG with its deletion mutants reveals that the N-terminal beta-sheet is essential for maintaining the folding topology and consequently maintaining the active-site structure of CcmG. Pro144 and Glu145 are key residues of the fingerprint region of CcmG. Pro144 is in cis-configuration, and it makes van der Waals interactions with the active-site disulfide Cys80-Cys83 and forms a C--H...O hydrogen bond with Thr82, helping stabilize the active-site structure. Glu145 forms a salt-bridge and hydrogen-bond network with other residues of the fingerprint region and with Arg158, further stabilizing the active-site structure. The cis-configuration of Pro144 makes the backbone nitrogen and oxygen of Ala143 exposed to solvent, favorable for interacting with binding partners. The key role of cis-Pro144 is verified by the P144A mutant, which contains trans-Ala144 and displays redox property changes. Structural comparison of E. coli CcmG with the recently reported structure of CcmG in complex with the N-terminal domain of DsbD reveals that Tyr141 undergoes conformational changes upon binding DsbD. A cis-proline located at the N-terminus of the first beta-strand of the betabetaalpha motif of the thioredoxin-like domain is a conserved structural feature of the thioredoxin superfamily.

About this StructureAbout this Structure

2B1K is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structures of E. coli CcmG and its mutants reveal key roles of the N-terminal beta-sheet and the fingerprint region., Ouyang N, Gao YG, Hu HY, Xia ZX, Proteins. 2006 Dec 1;65(4):1021-31. PMID:17019698 Page seeded by OCA on Sat May 3 19:44:22 2008

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