1vrs

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==Crystal structure of the disulfide-linked complex between the N-terminal and C-terminal domain of the electron transfer catalyst DsbD==
==Crystal structure of the disulfide-linked complex between the N-terminal and C-terminal domain of the electron transfer catalyst DsbD==
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<StructureSection load='1vrs' size='340' side='right' caption='[[1vrs]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
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<StructureSection load='1vrs' size='340' side='right'caption='[[1vrs]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1vrs]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecow3 Ecow3]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1se1 1se1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VRS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1VRS FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1vrs]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_str._K-12_substr._W3110 Escherichia coli str. K-12 substr. W3110]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1se1 1se1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VRS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VRS FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DSBD, DIPZ, CYCZ, CUTA2, B4136 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=316407 ECOW3])</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]] 2.85&#8491;</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-disulfide_reductase Protein-disulfide reductase], with EC number [http://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=1vrs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vrs OCA], [https://pdbe.org/1vrs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vrs RCSB], [https://www.ebi.ac.uk/pdbsum/1vrs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vrs ProSAT]</span></td></tr>
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<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=1vrs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vrs OCA], [http://pdbe.org/1vrs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1vrs RCSB], [http://www.ebi.ac.uk/pdbsum/1vrs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1vrs ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://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]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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==See Also==
==See Also==
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*[[Thiol:disulfide interchange protein|Thiol:disulfide interchange protein]]
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*[[Thiol:disulfide interchange protein 3D structures|Thiol:disulfide interchange protein 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Ecow3]]
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[[Category: Escherichia coli str. K-12 substr. W3110]]
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[[Category: Protein-disulfide reductase]]
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[[Category: Large Structures]]
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[[Category: Brunisholz, R]]
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[[Category: Brunisholz R]]
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[[Category: Capitani, G]]
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[[Category: Capitani G]]
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[[Category: Frei, P]]
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[[Category: Frei P]]
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[[Category: Glockshuber, R]]
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[[Category: Glockshuber R]]
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[[Category: Grauschopf, U]]
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[[Category: Grauschopf U]]
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[[Category: Gruetter, M G]]
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[[Category: Gruetter MG]]
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[[Category: Rozhkova, A]]
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[[Category: Rozhkova A]]
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[[Category: Stirnimann, C U]]
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[[Category: Stirnimann CU]]
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[[Category: Disulfide-linked]]
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[[Category: Dsbd]]
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[[Category: Immunoglobulin-like]]
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[[Category: Oxidoreductase]]
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[[Category: Thioredoxin-like]]
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Current revision

Crystal structure of the disulfide-linked complex between the N-terminal and C-terminal domain of the electron transfer catalyst DsbD

PDB ID 1vrs

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