1ht1: Difference between revisions

Latest revision as of 07:30, 7 February 2024

Nucleotide-Dependent Conformational Changes in a Protease-Associated ATPase HslU

Structural highlights

1ht1 is a 12 chain structure with sequence from Escherichia coli BL21(DE3). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.8Å
Ligands:	ADP
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HSLV_ECOLI Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. The complex has been shown to be involved in the specific degradation of heat shock induced transcription factors such as RpoH and SulA. In addition, small hydrophobic peptides are also hydrolyzed by HslV. HslV has weak protease activity even in the absence of HslU, but this activity is induced more than 100-fold in the presence of HslU. HslU recognizes protein substrates and unfolds these before guiding them to HslV for hydrolysis. HslV is not believed to degrade folded proteins.^[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.

References

↑ 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
↑ 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
↑ 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
↑ 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
↑ 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
↑ 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
↑ 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

Proteopedia Page Contributors and Editors (what is this?)

OCA

[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

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@@ Line 1: / Line 1: @@
-{{STRUCTURE_1ht1|  PDB=1ht1  |  SCENE=  }}
-===Nucleotide-Dependent Conformational Changes in a Protease-Associated ATPase HslU===
-{{ABSTRACT_PUBMED_11709174}}
-==Function==
+==Nucleotide-Dependent Conformational Changes in a Protease-Associated ATPase HslU==
-[[http://www.uniprot.org/uniprot/HSLV_ECOLI HSLV_ECOLI]] Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. The complex has been shown to be involved in the specific degradation of heat shock induced transcription factors such as RpoH and SulA. In addition, small hydrophobic peptides are also hydrolyzed by HslV. HslV has weak protease activity even in the absence of HslU, but this activity is induced more than 100-fold in the presence of HslU. HslU recognizes protein substrates and unfolds these before guiding them to HslV for hydrolysis. HslV is not believed to degrade folded proteins.<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>  [[http://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>
+<StructureSection load='1ht1' size='340' side='right'caption='[[1ht1]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1ht1]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_BL21(DE3) Escherichia coli BL21(DE3)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HT1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HT1 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]] 2.8&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</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=1ht1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ht1 OCA], [https://pdbe.org/1ht1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ht1 RCSB], [https://www.ebi.ac.uk/pdbsum/1ht1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ht1 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/HSLV_ECOLI HSLV_ECOLI] Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. The complex has been shown to be involved in the specific degradation of heat shock induced transcription factors such as RpoH and SulA. In addition, small hydrophobic peptides are also hydrolyzed by HslV. HslV has weak protease activity even in the absence of HslU, but this activity is induced more than 100-fold in the presence of HslU. HslU recognizes protein substrates and unfolds these before guiding them to HslV for hydrolysis. HslV is not believed to degrade folded proteins.<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/ht/1ht1_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=1ht1 ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-[[1ht1]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_bl21(de3) Escherichia coli bl21(de3)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HT1 OCA].
+*[[Heat Shock Protein structures|Heat Shock Protein structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:011709174</ref><references group="xtra"/><references/>
+__TOC__
-[[Category: Chung, C H.]]
+</StructureSection>
-[[Category: Eom, S H.]]
+[[Category: Large Structures]]
-[[Category: Franklin, M C.]]
+[[Category: Chung CH]]
-[[Category: Kamtekar, S.]]
+[[Category: Eom SH]]
-[[Category: Seong, I S.]]
+[[Category: Franklin MC]]
-[[Category: Song, J J.]]
+[[Category: Kamtekar S]]
-[[Category: Wang, J.]]
+[[Category: Seong IS]]
-[[Category: Chaperone]]
+[[Category: Song JJ]]
-[[Category: Hslvu]]
+[[Category: Wang J]]
-[[Category: Peptidase-atpase complex]]

1ht1: Difference between revisions

Latest revision as of 07:30, 7 February 2024

Nucleotide-Dependent Conformational Changes in a Protease-Associated ATPase HslU

Structural highlights

Function

Evolutionary Conservation

See Also

References

Contents

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