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New page: left|200px<br /><applet load="1uc7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1uc7, resolution 1.9Å" /> '''Crystal structure of ...
 
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[[Image:1uc7.jpg|left|200px]]<br /><applet load="1uc7" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1uc7, resolution 1.9&Aring;" />
'''Crystal structure of DsbDgamma'''<br />


==Overview==
==Crystal structure of DsbDgamma==
The Escherichia coli transmembrane protein DsbD transfers electrons from, the cytoplasm to the periplasm through a cascade of thiol-disulfide, exchange reactions. In this process, the C-terminal periplasmic domain of, DsbD (DsbDgamma) shuttles the reducing potential from the membrane domain, (DsbDbeta) to the N-terminal periplasmic domain (DsbDalpha). The crystal, structure of DsbDgamma determined at 1.9 A resolution reveals that the, domain has a thioredoxin fold with an extended N-terminal stretch. In, comparison to thioredoxin, the DsbDgamma structure exhibits the stabilized, active site conformation and the extended active site alpha2 helix that, explain the domain's substrate specificity and the redox potential shift, respectively. The hypothetical model of the DsbDgamma:DsbDalpha complex, based on the DsbDgamma structure and previous structural studies indicates, that the conserved hydrophobic residue in the C-X-X-C motif of DsbDgamma, may be important in the specific recognition of DsbDalpha.
<StructureSection load='1uc7' size='340' side='right'caption='[[1uc7]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1uc7]] is a 2 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=1UC7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UC7 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]] 1.9&#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=1uc7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uc7 OCA], [https://pdbe.org/1uc7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uc7 RCSB], [https://www.ebi.ac.uk/pdbsum/1uc7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uc7 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DSBD_ECO57 DSBD_ECO57] 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. This transfer involves a cascade of disulfide bond formation and reduction steps (By similarity).
== 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/uc/1uc7_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=1uc7 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The Escherichia coli transmembrane protein DsbD transfers electrons from the cytoplasm to the periplasm through a cascade of thiol-disulfide exchange reactions. In this process, the C-terminal periplasmic domain of DsbD (DsbDgamma) shuttles the reducing potential from the membrane domain (DsbDbeta) to the N-terminal periplasmic domain (DsbDalpha). The crystal structure of DsbDgamma determined at 1.9 A resolution reveals that the domain has a thioredoxin fold with an extended N-terminal stretch. In comparison to thioredoxin, the DsbDgamma structure exhibits the stabilized active site conformation and the extended active site alpha2 helix that explain the domain's substrate specificity and the redox potential shift, respectively. The hypothetical model of the DsbDgamma:DsbDalpha complex based on the DsbDgamma structure and previous structural studies indicates that the conserved hydrophobic residue in the C-X-X-C motif of DsbDgamma may be important in the specific recognition of DsbDalpha.


==About this Structure==
Crystal structure of DsbDgamma reveals the mechanism of redox potential shift and substrate specificity(1).,Kim JH, Kim SJ, Jeong DG, Son JH, Ryu SE FEBS Lett. 2003 May 22;543(1-3):164-9. PMID:12753926<ref>PMID:12753926</ref>
1UC7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UC7 OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Crystal structure of DsbDgamma reveals the mechanism of redox potential shift and substrate specificity(1)., Kim JH, Kim SJ, Jeong DG, Son JH, Ryu SE, FEBS Lett. 2003 May 22;543(1-3):164-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12753926 12753926]
</div>
<div class="pdbe-citations 1uc7" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Thiol:disulfide interchange protein 3D structures|Thiol:disulfide interchange protein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Protein-disulfide reductase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Jeong DG]]
[[Category: Jeong, D.G.]]
[[Category: Kim JH]]
[[Category: Kim, J.H.]]
[[Category: Kim SJ]]
[[Category: Kim, S.J.]]
[[Category: Ryu SE]]
[[Category: Ryu, S.E.]]
[[Category: Son JH]]
[[Category: Son, J.H.]]
[[Category: thioredoxin-fold]]
 
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