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2b1l

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[[Image:2b1l.jpg|left|200px]]
 
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==Crystal structure of N-terminal 57 residue deletion mutant of E. coli CcmG protein(residues 58-185)==
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The line below this paragraph, containing "STRUCTURE_2b1l", creates the "Structure Box" on the page.
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<StructureSection load='2b1l' size='340' side='right'caption='[[2b1l]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2b1l]] is a 2 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=2B1L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2B1L FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2b1l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b1l OCA], [https://pdbe.org/2b1l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b1l RCSB], [https://www.ebi.ac.uk/pdbsum/2b1l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b1l ProSAT]</span></td></tr>
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{{STRUCTURE_2b1l| PDB=2b1l | SCENE= }}
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b1/2b1l_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2b1l ConSurf].
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<div style="clear:both"></div>
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'''Crystal structure of N-terminal 57 residue deletion mutant of E. coli CcmG protein(residues 58-185)'''
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==See Also==
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*[[Thiol:disulfide interchange protein 3D structures|Thiol:disulfide interchange protein 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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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.
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==About this Structure==
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2B1L is a [[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=2B1L OCA].
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/17019698 17019698]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Gao, Y G.]]
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[[Category: Gao YG]]
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[[Category: Hu, H Y.]]
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[[Category: Hu HY]]
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[[Category: Ouyang, N.]]
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[[Category: Ouyang N]]
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[[Category: Xia, Z X.]]
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[[Category: Xia ZX]]
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[[Category: Comparison with the e coli ccmg]]
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[[Category: Folding topology change]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:44:22 2008''
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Current revision

Crystal structure of N-terminal 57 residue deletion mutant of E. coli CcmG protein(residues 58-185)

PDB ID 2b1l

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