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[[Image:1t3b.gif|left|200px]]


{{Structure
==X-ray Structure of DsbC from Haemophilus influenzae==
|PDB= 1t3b |SIZE=350|CAPTION= <scene name='initialview01'>1t3b</scene>, resolution 2.5&Aring;
<StructureSection load='1t3b' size='340' side='right'caption='[[1t3b]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<table><tr><td colspan='2'>[[1t3b]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T3B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1T3B FirstGlance]. <br>
|ACTIVITY= [http://en.wikipedia.org/wiki/Protein_disulfide-isomerase Protein disulfide-isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.4.1 5.3.4.1]  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
|GENE= DSBC, XPRA, HI1213 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=727 Haemophilus influenzae])
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1t3b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t3b OCA], [https://pdbe.org/1t3b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t3b RCSB], [https://www.ebi.ac.uk/pdbsum/1t3b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t3b ProSAT]</span></td></tr>
}}
</table>
== Function ==
[https://www.uniprot.org/uniprot/DSBC_HAEIN DSBC_HAEIN] Required for disulfide bond formation in some periplasmic proteins. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbC is reoxidized by a yet uncharacterized protein. Also acts as a disulfide isomerase (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/t3/1t3b_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=1t3b ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Bacterial DsbC proteins are involved in rearranging or reducing mismatched disulfide bonds folding within the periplasm. The X-ray structure of the enzyme from Haemophilus influenzae has been solved and compared with the known structure of the Escherichia coli protein. The proteins act as V-shaped dimers with a large cleft to accommodate substrate proteins. The dimers are anchored by a small N-terminal domain, but have a flexible linker region which allows the larger C-terminal domain, with its reactive sulfhydryls, to clamp down on substrates. The overall folds are very similar, but the comparison shows a wider range of hinge motions than previously thought. The crystal packing of the H. influenzae protein allows the movement of the N-terminal domain with respect to the C-terminal domain through motions in the flexible hinge, generating high thermal parameters and unusually high anisotropy in the crystallographic data.


'''X-ray Structure of DsbC from Haemophilus influenzae'''
Structure of DsbC from Haemophilus influenzae.,Zhang M, Monzingo AF, Segatori L, Georgiou G, Robertus JD Acta Crystallogr D Biol Crystallogr. 2004 Sep;60(Pt 9):1512-8. Epub 2004, Aug 26. PMID:15333920<ref>PMID:15333920</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1t3b" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
Bacterial DsbC proteins are involved in rearranging or reducing mismatched disulfide bonds folding within the periplasm. The X-ray structure of the enzyme from Haemophilus influenzae has been solved and compared with the known structure of the Escherichia coli protein. The proteins act as V-shaped dimers with a large cleft to accommodate substrate proteins. The dimers are anchored by a small N-terminal domain, but have a flexible linker region which allows the larger C-terminal domain, with its reactive sulfhydryls, to clamp down on substrates. The overall folds are very similar, but the comparison shows a wider range of hinge motions than previously thought. The crystal packing of the H. influenzae protein allows the movement of the N-terminal domain with respect to the C-terminal domain through motions in the flexible hinge, generating high thermal parameters and unusually high anisotropy in the crystallographic data.
*[[Thiol:disulfide interchange protein 3D structures|Thiol:disulfide interchange protein 3D structures]]
 
== References ==
==About this Structure==
<references/>
1T3B is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T3B OCA].
__TOC__
 
</StructureSection>
==Reference==
Structure of DsbC from Haemophilus influenzae., Zhang M, Monzingo AF, Segatori L, Georgiou G, Robertus JD, Acta Crystallogr D Biol Crystallogr. 2004 Sep;60(Pt 9):1512-8. Epub 2004, Aug 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15333920 15333920]
[[Category: Haemophilus influenzae]]
[[Category: Haemophilus influenzae]]
[[Category: Protein disulfide-isomerase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Georgiou G]]
[[Category: Georgiou, G.]]
[[Category: Monzingo AF]]
[[Category: Monzingo, A F.]]
[[Category: Robertus JD]]
[[Category: Robertus, J D.]]
[[Category: Segatori L]]
[[Category: Segatori, L.]]
[[Category: Zhang M]]
[[Category: Zhang, M.]]
[[Category: oxidoreductase]]
[[Category: protein disulfide isomerase]]
[[Category: protein folding]]
[[Category: redox protein]]
[[Category: redox-active center]]
 
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