2b1k: Difference between revisions

New page: left|200px<br /><applet load="2b1k" size="450" color="white" frame="true" align="right" spinBox="true" caption="2b1k, resolution 1.90Å" /> '''Crystal structure of...
 
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caption="2b1k, resolution 1.90&Aring;" />
caption="2b1k, resolution 1.90&Aring;" />
'''Crystal structure of E. coli CcmG protein'''<br />
'''Crystal structure of E. coli CcmG protein'''<br />


==Overview==
==Overview==
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.
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 Structure==
==About this Structure==
2B1K is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2B1K OCA].  
2B1K is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B1K OCA].  


==Reference==
==Reference==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Gao, Y.G.]]
[[Category: Gao, Y G.]]
[[Category: Hu, H.Y.]]
[[Category: Hu, H Y.]]
[[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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