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3pfu

From Proteopedia

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Current revision (17:06, 1 November 2023) (edit) (undo)
 
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<StructureSection load='3pfu' size='340' side='right'caption='[[3pfu]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='3pfu' size='340' side='right'caption='[[3pfu]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3pfu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PFU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PFU FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3pfu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PFU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PFU FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DTT:2,3-DIHYDROXY-1,4-DITHIOBUTANE'>DTT</scene></td></tr>
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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]] 1.8&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1l6p|1l6p]], [[1jpe|1jpe]], [[1vrs|1vrs]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DTT:2,3-DIHYDROXY-1,4-DITHIOBUTANE'>DTT</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dsbD, cutA2, cycZ, dipZ, b4136, JW5734 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Protein-disulfide_reductase Protein-disulfide reductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.8 1.8.1.8] </span></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=3pfu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pfu OCA], [https://pdbe.org/3pfu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pfu RCSB], [https://www.ebi.ac.uk/pdbsum/3pfu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pfu ProSAT]</span></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=3pfu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pfu OCA], [https://pdbe.org/3pfu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pfu RCSB], [https://www.ebi.ac.uk/pdbsum/3pfu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pfu ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/DSBD_ECOLI DSBD_ECOLI]] Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm, thereby maintaining the active site of DsbC, DsbE and DsbG in a reduced state. This transfer involves a cascade of disulfide bond formation and reduction steps.[HAMAP-Rule:MF_00399]
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[https://www.uniprot.org/uniprot/DSBD_ECOLI DSBD_ECOLI] Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm, thereby maintaining the active site of DsbC, DsbE and DsbG in a reduced state. This transfer involves a cascade of disulfide bond formation and reduction steps.[HAMAP-Rule:MF_00399]
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Ecoli]]
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[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Protein-disulfide reductase]]
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[[Category: Ferguson SJ]]
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[[Category: Ferguson, S J]]
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[[Category: Mavridou DAI]]
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[[Category: Mavridou, D A.I]]
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[[Category: Redfield C]]
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[[Category: Redfield, C]]
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[[Category: Saridakis E]]
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[[Category: Saridakis, E]]
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[[Category: Electron transport]]
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[[Category: Immunoglobulin-like fold]]
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[[Category: Oxidoreductase]]
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[[Category: Periplasmic domain of transmembrane protein]]
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[[Category: Thiol disulfide oxidoreductase]]
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Current revision

N-terminal domain of Thiol:disulfide interchange protein DsbD in its reduced form

PDB ID 3pfu

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OCA

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