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| | ==Crystal Structure of P144A mutant of E.coli CcmG protein== | | ==Crystal Structure of P144A mutant of E.coli CcmG protein== |
| - | <StructureSection load='2g0f' size='340' side='right' caption='[[2g0f]], [[Resolution|resolution]] 2.20Å' scene=''> | + | <StructureSection load='2g0f' size='340' side='right'caption='[[2g0f]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2g0f]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G0F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2G0F FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2g0f]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G0F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2G0F FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2b1k|2b1k]], [[2b1l|2b1l]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ccmG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2g0f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2g0f OCA], [https://pdbe.org/2g0f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2g0f RCSB], [https://www.ebi.ac.uk/pdbsum/2g0f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2g0f ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2g0f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2g0f OCA], [http://pdbe.org/2g0f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2g0f RCSB], [http://www.ebi.ac.uk/pdbsum/2g0f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2g0f ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/DSBE_ECOLI DSBE_ECOLI]] Involved in disulfide bond formation. Catalyzes a late, reductive step in the assembly of periplasmic c-type cytochromes, probably the reduction of disulfide bonds of the apocytochrome c to allow covalent linkage with the heme. Possible subunit of a heme lyase. DsbE is maintained in a reduced state by DsbD. | + | [https://www.uniprot.org/uniprot/DSBE_ECOLI DSBE_ECOLI] Involved in disulfide bond formation. Catalyzes a late, reductive step in the assembly of periplasmic c-type cytochromes, probably the reduction of disulfide bonds of the apocytochrome c to allow covalent linkage with the heme. Possible subunit of a heme lyase. DsbE is maintained in a reduced state by DsbD. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g0/2g0f_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g0/2g0f_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | ==See Also== | | ==See Also== |
| - | *[[Thiol:disulfide interchange protein|Thiol:disulfide interchange protein]] | + | *[[Thiol:disulfide interchange protein 3D structures|Thiol:disulfide interchange protein 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| - | [[Category: Gao, Y G]] | + | [[Category: Large Structures]] |
| - | [[Category: Hu, H Y]] | + | [[Category: Gao YG]] |
| - | [[Category: Ouyang, N]] | + | [[Category: Hu HY]] |
| - | [[Category: Xia, Z X]] | + | [[Category: Ouyang N]] |
| - | [[Category: Cis-to-trans configuration change]] | + | [[Category: Xia ZX]] |
| - | [[Category: E coli ccmg]]
| + | |
| - | [[Category: Oxidoreductase]]
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| - | [[Category: P144a mutant]]
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| Structural highlights
Function
DSBE_ECOLI Involved in disulfide bond formation. Catalyzes a late, reductive step in the assembly of periplasmic c-type cytochromes, probably the reduction of disulfide bonds of the apocytochrome c to allow covalent linkage with the heme. Possible subunit of a heme lyase. DsbE is maintained in a reduced state by DsbD.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ouyang N, Gao YG, Hu HY, Xia ZX. Crystal structures of E. coli CcmG and its mutants reveal key roles of the N-terminal beta-sheet and the fingerprint region. Proteins. 2006 Dec 1;65(4):1021-31. PMID:17019698 doi:10.1002/prot.21184
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