1un2

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[[Image:1un2.png|left|200px]]
 
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==Crystal structure of circularly permuted CPDSBA_Q100T99: Preserved Global Fold and Local Structural Adjustments==
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The line below this paragraph, containing "STRUCTURE_1un2", creates the "Structure Box" on the page.
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<StructureSection load='1un2' size='340' side='right'caption='[[1un2]], [[Resolution|resolution]] 2.40&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'>[[1un2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1dyv 1dyv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UN2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UN2 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]] 2.4&#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=1un2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1un2 OCA], [https://pdbe.org/1un2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1un2 RCSB], [https://www.ebi.ac.uk/pdbsum/1un2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1un2 ProSAT]</span></td></tr>
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{{STRUCTURE_1un2| PDB=1un2 | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/DSBA_ECOLI DSBA_ECOLI] Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbA is reoxidized by DsbB. Required for pilus biogenesis. PhoP-regulated transcription is redox-sensitive, being activated when the periplasm becomes more reducing (deletion of dsbA/dsbB, treatment with dithiothreitol). MgrB acts between DsbA/DsbB and PhoP/PhoQ in this pathway.<ref>PMID:1429594</ref> <ref>PMID:22267510</ref>
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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/un/1un2_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=1un2 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The thiol-disulfide oxidoreductase DsbA is required for efficient formation of disulfide bonds in the Escherichia coli periplasm. The enzyme is the strongest oxidant of the family of thioredoxin-like proteins and three-dimensional structures of both oxidized and reduced forms are known. DsbA consists of a catalytic thioredoxin-like domain and a helical domain that is inserted into the thioredoxin motif. Here, the X-ray structure of a circularly permuted variant, cpDsbA(Q100T99), is reported in which the natural termini are joined by the pentapeptide linker GGGTG, leading to a continuous thioredoxin domain, and new termini that have been introduced in the helical domain by breaking the peptide bond Thr99-Gln100. cpDsbA(Q100T99) is catalytically active in vivo and in vitro. The crystal structure of oxidized cpDsbA(Q100T99), determined by molecular replacement at 2.4 A resolution, was found to be very similar to that of wild-type DsbA. The lower thermodynamic stability of cpDsbA(Q100T99) relative to DsbA is associated with small structural changes within the molecule, especially near the new termini and the circularizing linker. The active-site helices and adjacent loops display increased flexibility compared with oxidized DsbA.
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===CRYSTAL STRUCTURE OF CIRCULARLY PERMUTED CPDSBA_Q100T99 PRESERVED GLOBAL FOLD AND LOCAL STRUCTURAL ADJUSTMENTS===
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Structure of circularly permuted DsbA(Q100T99): preserved global fold and local structural adjustments.,Manjasetty BA, Hennecke J, Glockshuber R, Heinemann U Acta Crystallogr D Biol Crystallogr. 2004 Feb;60(Pt 2):304-9. Epub 2004, Jan 23. PMID:14747707<ref>PMID:14747707</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_14747707}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1un2" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 14747707 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_14747707}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[1un2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1dyv 1dyv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UN2 OCA].
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==Reference==
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<ref group="xtra">PMID:14747707</ref><ref group="xtra">PMID:10047491</ref><references group="xtra"/>
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Glockshuber, R.]]
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[[Category: Large Structures]]
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[[Category: Heinemann, U.]]
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[[Category: Glockshuber R]]
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[[Category: Hennecke, J.]]
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[[Category: Heinemann U]]
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[[Category: Manjasetty, B A.]]
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[[Category: Hennecke J]]
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[[Category: Circular permutation]]
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[[Category: Manjasetty BA]]
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[[Category: Disulfide bond formation]]
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[[Category: Disulfide oxidoreductase]]
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[[Category: Oxidoreductase]]
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[[Category: Protein disulfide isomerase]]
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[[Category: Protein folding]]
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[[Category: Redox protein]]
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[[Category: Thioredoxin]]
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Current revision

Crystal structure of circularly permuted CPDSBA_Q100T99: Preserved Global Fold and Local Structural Adjustments

PDB ID 1un2

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