1t3b
From Proteopedia
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| - | [[Image:1t3b.gif|left|200px]]<br /><applet load="1t3b" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1t3b, resolution 2.5Å" /> | ||
| - | '''X-ray Structure of DsbC from Haemophilus influenzae'''<br /> | ||
| - | == | + | ==X-ray Structure of DsbC from Haemophilus influenzae== |
| + | <StructureSection load='1t3b' size='340' side='right'caption='[[1t3b]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <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> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</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=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. | 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. | ||
| - | + | 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> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1t3b" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Thiol:disulfide interchange protein 3D structures|Thiol:disulfide interchange protein 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Haemophilus influenzae]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Georgiou G]] | ||
| + | [[Category: Monzingo AF]] | ||
| + | [[Category: Robertus JD]] | ||
| + | [[Category: Segatori L]] | ||
| + | [[Category: Zhang M]] | ||
Current revision
X-ray Structure of DsbC from Haemophilus influenzae
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