2zuq
From Proteopedia
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- | {{Seed}} | ||
- | [[Image:2zuq.png|left|200px]] | ||
- | < | + | ==Crystal structure of DsbB-Fab complex== |
- | + | <StructureSection load='2zuq' size='340' side='right'caption='[[2zuq]], [[Resolution|resolution]] 3.30Å' scene=''> | |
- | You may | + | == Structural highlights == |
- | + | <table><tr><td colspan='2'>[[2zuq]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZUQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZUQ FirstGlance]. <br> | |
- | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.3Å</td></tr> | |
- | -- | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=UQ1:UBIQUINONE-1'>UQ1</scene></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=2zuq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zuq OCA], [https://pdbe.org/2zuq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zuq RCSB], [https://www.ebi.ac.uk/pdbsum/2zuq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zuq ProSAT]</span></td></tr> | |
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/DSBB_ECOLI DSBB_ECOLI] Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by oxidizing the DsbA protein.<ref>PMID:8430071</ref> <ref>PMID:7688471</ref> | ||
+ | == Evolutionary Conservation == | ||
+ | [[Image:Consurf_key_small.gif|200px|right]] | ||
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zu/2zuq_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </jmolCheckbox> | ||
+ | </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=2zuq ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | In the Escherichia coli system catalysing oxidative protein folding, disulphide bonds are generated by the cooperation of DsbB and ubiquinone and transferred to substrate proteins through DsbA. The structures solved so far for different forms of DsbB lack the Cys104-Cys130 initial-state disulphide that is directly donated to DsbA. Here, we report the 3.4 A crystal structure of a DsbB-Fab complex, in which DsbB has this principal disulphide. Its comparison with the updated structure of the DsbB-DsbA complex as well as with the recently reported NMR structure of a DsbB variant having the rearranged Cys41-Cys130 disulphide illuminated conformational transitions of DsbB induced by the binding and release of DsbA. Mutational studies revealed that the membrane-parallel short alpha-helix of DsbB has a key function in physiological electron flow, presumably by controlling the positioning of the Cys130-containing loop. These findings demonstrate that DsbB has developed the elaborate conformational dynamism to oxidize DsbA for continuous protein disulphide bond formation in the cell. | ||
- | + | Dynamic nature of disulphide bond formation catalysts revealed by crystal structures of DsbB.,Inaba K, Murakami S, Nakagawa A, Iida H, Kinjo M, Ito K, Suzuki M EMBO J. 2009 Mar 18;28(6):779-91. Epub 2009 Feb 12. PMID:19214188<ref>PMID:19214188</ref> | |
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 2zuq" style="background-color:#fffaf0;"></div> | ||
- | + | ==See Also== | |
- | + | *[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]] | |
- | + | *[[Thiol:disulfide interchange protein 3D structures|Thiol:disulfide interchange protein 3D structures]] | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | == | + | </StructureSection> |
- | + | [[Category: Escherichia coli K-12]] | |
- | + | [[Category: Large Structures]] | |
- | == | + | |
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- | [[Category: Escherichia coli]] | + | |
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
- | [[Category: Inaba | + | [[Category: Inaba K]] |
- | [[Category: Murakami | + | [[Category: Murakami S]] |
- | [[Category: Suzuki | + | [[Category: Suzuki M]] |
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Current revision
Crystal structure of DsbB-Fab complex
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