1g4a: Difference between revisions

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New page: left|200px<br /><applet load="1g4a" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g4a, resolution 3.00Å" /> '''CRYSTAL STRUCTURES O...
 
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[[Image:1g4a.jpg|left|200px]]<br /><applet load="1g4a" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1g4a, resolution 3.00&Aring;" />
'''CRYSTAL STRUCTURES OF THE HSLVU PEPTIDASE-ATPASE COMPLEX REVEAL AN ATP-DEPENDENT PROTEOLYSIS MECHANISM'''<br />


==Overview==
==CRYSTAL STRUCTURES OF THE HSLVU PEPTIDASE-ATPASE COMPLEX REVEAL AN ATP-DEPENDENT PROTEOLYSIS MECHANISM==
BACKGROUND: The bacterial heat shock locus HslU ATPase and HslV peptidase, together form an ATP-dependent HslVU protease. Bacterial HslVU is a, homolog of the eukaryotic 26S proteasome. Crystallographic studies of, HslVU should provide an understanding of ATP-dependent protein unfolding, translocation, and proteolysis by this and other ATP-dependent proteases., RESULTS: We present a 3.0 A resolution crystal structure of HslVU with an, HslU hexamer bound at one end of an HslV dodecamer. The structure shows, that the central pores of the ATPase and peptidase are next to each other, and aligned. The central pore of HslU consists of a GYVG motif, which is, conserved among protease-associated ATPases. The binding of one HslU, hexamer to one end of an HslV dodecamer in the 3.0 A resolution structure, opens both HslV central pores and induces asymmetric changes in HslV., CONCLUSIONS: Analysis of nucleotide binding induced conformational changes, in the current and previous HslU structures suggests a protein, unfolding-coupled translocation mechanism. In this mechanism, unfolded, polypeptides are threaded through the aligned pores of the ATPase and, peptidase and translocated into the peptidase central chamber.
<StructureSection load='1g4a' size='340' side='right'caption='[[1g4a]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1g4a]] is a 6 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=1G4A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G4A 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]] 3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DAT:2-DEOXYADENOSINE-5-DIPHOSPHATE'>DAT</scene></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=1g4a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g4a OCA], [https://pdbe.org/1g4a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g4a RCSB], [https://www.ebi.ac.uk/pdbsum/1g4a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g4a ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HSLU_ECOLI HSLU_ECOLI] ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.<ref>PMID:8662828</ref> <ref>PMID:8650174</ref> <ref>PMID:9288941</ref> <ref>PMID:9393683</ref> <ref>PMID:10452560</ref> <ref>PMID:10419524</ref> <ref>PMID:15696175</ref>
== 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/g4/1g4a_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=1g4a ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1G4A is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with DAT as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1G4A OCA].
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
 
== References ==
==Reference==
<references/>
Crystal structures of the HslVU peptidase-ATPase complex reveal an ATP-dependent proteolysis mechanism., Wang J, Song JJ, Franklin MC, Kamtekar S, Im YJ, Rho SH, Seong IS, Lee CS, Chung CH, Eom SH, Structure. 2001 Feb 7;9(2):177-84. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11250202 11250202]
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Chung, C.H.]]
[[Category: Chung CH]]
[[Category: Eom, S.H.]]
[[Category: Eom SH]]
[[Category: Franklin, M.C.]]
[[Category: Franklin MC]]
[[Category: Im, Y.J.]]
[[Category: Im YJ]]
[[Category: Kamtekar, S.]]
[[Category: Kamtekar S]]
[[Category: Lee, C.S.]]
[[Category: Lee CS]]
[[Category: Rho, S.H.]]
[[Category: Rho SH]]
[[Category: Seong, I.S.]]
[[Category: Seong IS]]
[[Category: Song, J.J.]]
[[Category: Song JJ]]
[[Category: Wang, J.]]
[[Category: Wang J]]
[[Category: DAT]]
[[Category: hslvu]]
[[Category: peptidase-atpase complex]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:41:25 2007''

Latest revision as of 10:22, 7 February 2024

CRYSTAL STRUCTURES OF THE HSLVU PEPTIDASE-ATPASE COMPLEX REVEAL AN ATP-DEPENDENT PROTEOLYSIS MECHANISMCRYSTAL STRUCTURES OF THE HSLVU PEPTIDASE-ATPASE COMPLEX REVEAL AN ATP-DEPENDENT PROTEOLYSIS MECHANISM

Structural highlights

1g4a is a 6 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 3Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HSLU_ECOLI ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.[1] [2] [3] [4] [5] [6] [7]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Yoo SJ, Seol JH, Shin DH, Rohrwild M, Kang MS, Tanaka K, Goldberg AL, Chung CH. Purification and characterization of the heat shock proteins HslV and HslU that form a new ATP-dependent protease in Escherichia coli. J Biol Chem. 1996 Jun 14;271(24):14035-40. PMID:8662828
  2. ↑ Rohrwild M, Coux O, Huang HC, Moerschell RP, Yoo SJ, Seol JH, Chung CH, Goldberg AL. HslV-HslU: A novel ATP-dependent protease complex in Escherichia coli related to the eukaryotic proteasome. Proc Natl Acad Sci U S A. 1996 Jun 11;93(12):5808-13. PMID:8650174
  3. ↑ Seol JH, Yoo SJ, Shin DH, Shim YK, Kang MS, Goldberg AL, Chung CH. The heat-shock protein HslVU from Escherichia coli is a protein-activated ATPase as well as an ATP-dependent proteinase. Eur J Biochem. 1997 Aug 1;247(3):1143-50. PMID:9288941
  4. ↑ Kanemori M, Nishihara K, Yanagi H, Yura T. Synergistic roles of HslVU and other ATP-dependent proteases in controlling in vivo turnover of sigma32 and abnormal proteins in Escherichia coli. J Bacteriol. 1997 Dec;179(23):7219-25. PMID:9393683
  5. ↑ Seong IS, Oh JY, Yoo SJ, Seol JH, Chung CH. ATP-dependent degradation of SulA, a cell division inhibitor, by the HslVU protease in Escherichia coli. FEBS Lett. 1999 Jul 30;456(1):211-4. PMID:10452560
  6. ↑ Kanemori M, Yanagi H, Yura T. Marked instability of the sigma(32) heat shock transcription factor at high temperature. Implications for heat shock regulation. J Biol Chem. 1999 Jul 30;274(31):22002-7. PMID:10419524
  7. ↑ Burton RE, Baker TA, Sauer RT. Nucleotide-dependent substrate recognition by the AAA+ HslUV protease. Nat Struct Mol Biol. 2005 Mar;12(3):245-51. Epub 2005 Feb 6. PMID:15696175 doi:10.1038/nsmb898

1g4a, resolution 3.00Å

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