1bg8: Difference between revisions

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[[Image:1bg8.gif|left|200px]]


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==HDEA FROM ESCHERICHIA COLI==
The line below this paragraph, containing "STRUCTURE_1bg8", creates the "Structure Box" on the page.
<StructureSection load='1bg8' size='340' side='right'caption='[[1bg8]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1bg8]] is a 3 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=1BG8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BG8 FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</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=1bg8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bg8 OCA], [https://pdbe.org/1bg8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bg8 RCSB], [https://www.ebi.ac.uk/pdbsum/1bg8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bg8 ProSAT]</span></td></tr>
{{STRUCTURE_1bg8|  PDB=1bg8 |  SCENE= }}
</table>
 
== Function ==
'''HDEA FROM ESCHERICHIA COLI'''
[https://www.uniprot.org/uniprot/HDEA_ECOLI HDEA_ECOLI] Required for optimal acid stress protection. Exhibits a chaperone-like activity only at pH below 3 by suppressing non-specifically the aggregation of denaturated periplasmic proteins. Important for survival of enteric bacteria in the acidic environment of the host stomach. Also promotes the solubilization at neutral pH of proteins that had aggregated in their presence at acidic pHs. May cooperate with other periplasmic chaperones such as DegP and SurA.<ref>PMID:15911614</ref> <ref>PMID:17085547</ref> <ref>PMID:18359765</ref> <ref>PMID:21892184</ref>
 
== References ==
 
<references/>
==About this Structure==
__TOC__
1BG8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BG8 OCA].  
</StructureSection>
 
==Reference==
Crystal structure of Escherichia coli HdeA., Yang F, Gustafson KR, Boyd MR, Wlodawer A, Nat Struct Biol. 1998 Sep;5(9):763-4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9731767 9731767]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Boyd, M R.]]
[[Category: Boyd MR]]
[[Category: Gustafson, K R.]]
[[Category: Gustafson KR]]
[[Category: Wlodawer, A.]]
[[Category: Wlodawer A]]
[[Category: Yang, F.]]
[[Category: Yang F]]
[[Category: Hdea]]
[[Category: Periplasmic]]
[[Category: Signal]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 11:28:24 2008''

Latest revision as of 02:49, 21 November 2024

HDEA FROM ESCHERICHIA COLIHDEA FROM ESCHERICHIA COLI

Structural highlights

1bg8 is a 3 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HDEA_ECOLI Required for optimal acid stress protection. Exhibits a chaperone-like activity only at pH below 3 by suppressing non-specifically the aggregation of denaturated periplasmic proteins. Important for survival of enteric bacteria in the acidic environment of the host stomach. Also promotes the solubilization at neutral pH of proteins that had aggregated in their presence at acidic pHs. May cooperate with other periplasmic chaperones such as DegP and SurA.[1] [2] [3] [4]

References

  1. ↑ Hong W, Jiao W, Hu J, Zhang J, Liu C, Fu X, Shen D, Xia B, Chang Z. Periplasmic protein HdeA exhibits chaperone-like activity exclusively within stomach pH range by transforming into disordered conformation. J Biol Chem. 2005 Jul 22;280(29):27029-34. Epub 2005 May 23. PMID:15911614 doi:http://dx.doi.org/M503934200
  2. ↑ Kern R, Malki A, Abdallah J, Tagourti J, Richarme G. Escherichia coli HdeB is an acid stress chaperone. J Bacteriol. 2007 Jan;189(2):603-10. Epub 2006 Nov 3. PMID:17085547 doi:http://dx.doi.org/10.1128/JB.01522-06
  3. ↑ Malki A, Le HT, Milles S, Kern R, Caldas T, Abdallah J, Richarme G. Solubilization of protein aggregates by the acid stress chaperones HdeA and HdeB. J Biol Chem. 2008 May 16;283(20):13679-87. Epub 2008 Mar 20. PMID:18359765 doi:http://dx.doi.org/M800869200
  4. ↑ Zhang M, Lin S, Song X, Liu J, Fu Y, Ge X, Fu X, Chang Z, Chen PR. A genetically incorporated crosslinker reveals chaperone cooperation in acid resistance. Nat Chem Biol. 2011 Sep 4;7(10):671-7. doi: 10.1038/nchembio.644. PMID:21892184 doi:http://dx.doi.org/10.1038/nchembio.644

1bg8, resolution 2.20Å

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