This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

1l6p

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

N-terminal of DsbD (residues 20-144) from E. coli.

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1l6p"

Categories: Escherichia coli | Large Structures | Goulding CW | Parseghian A | Sawaya MR

@@ Line 1: / Line 1: @@
-[[Image:1l6p.jpg|left|200px]]<br /><applet load="1l6p" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1l6p, resolution 1.65&Aring;" />
-'''N-terminal of DsbD (residues 20-144) from E. coli.'''<br />
-==Overview==
+==N-terminal of DsbD (residues 20-144) from E. coli.==
-Escherichia coli DsbD transports electrons across the plasma membrane, a, pathway that leads to the reduction of protein disulfide bonds. Three, secreted thioredoxin-like factors, DsbC, DsbE, and DsbG, reduce protein, disulfide bonds whereby an active site C-X-X-C motif is oxidized to, generate a disulfide bond. DsbD catalyzes the reduction of the disulfide, of DsbC, DsbE, and DsbG but not of the thioredoxin-like oxidant DsbA. The, reduction of DsbC, DsbE, and DsbG occurs by transport of electrons from, cytoplasmic thioredoxin to the C-terminal thioredoxin-like domain of DsbD, (DsbD(C)). The N-terminal domain of DsbD, DsbD(N), acts as a versatile, adaptor in electron transport and is capable of forming disulfides with, oxidized DsbC, DsbE, or DsbG as well as with reduced DsbD(C). Isolated, DsbD(N) is functional in electron transport in vitro. Crystallized DsbD(N), assumes an immunoglobulin-like fold that encompasses two active site, cysteines, C103 and C109, forming a disulfide bond between beta-strands., The disulfide of DsbD(N) is shielded from the environment and capped by a, phenylalanine (F70). A model is discussed whereby the immunoglobulin fold, of DsbD(N) may provide for the discriminating interaction with, thioredoxin-like factors, thereby triggering movement of the phenylalanine, cap followed by disulfide rearrangement.
+<StructureSection load='1l6p' size='340' side='right'caption='[[1l6p]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1l6p]] is a 1 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=1L6P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L6P 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]] 1.65&#8491;</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=1l6p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l6p OCA], [https://pdbe.org/1l6p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l6p RCSB], [https://www.ebi.ac.uk/pdbsum/1l6p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l6p ProSAT]</span></td></tr>
+</table>
+== Function ==
+[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 ==
+[[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/l6/1l6p_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1l6p ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-L6P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1L6P OCA].
+*[[Thiol:disulfide interchange protein 3D structures|Thiol:disulfide interchange protein 3D structures]]
+__TOC__
-==Reference==
+</StructureSection>
-Thiol-disulfide exchange in an immunoglobulin-like fold: structure of the N-terminal domain of DsbD., Goulding CW, Sawaya MR, Parseghian A, Lim V, Eisenberg D, Missiakas D, Biochemistry. 2002 Jun 4;41(22):6920-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12033924 12033924]
 [[Category: Escherichia coli]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Goulding, C.W.]]
+[[Category: Goulding CW]]
-[[Category: Parseghian, A.]]
+[[Category: Parseghian A]]
-[[Category: Sawaya, M.R.]]
+[[Category: Sawaya MR]]
-[[Category: disulfide bond isomerase protein]]
-[[Category: immunoglobulin-like fold]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:19:15 2007''

1l6p

From Proteopedia

Current revision

N-terminal of DsbD (residues 20-144) from E. coli.

Structural highlights

Function

Evolutionary Conservation

See Also

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox