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- | [[Image:1yyf.gif|left|200px]] | |
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- | {{Structure
| + | ==Correction of X-ray Intensities from an HslV-HslU co-crystal containing lattice translocation defects== |
- | |PDB= 1yyf |SIZE=350|CAPTION= <scene name='initialview01'>1yyf</scene>, resolution 4.16Å
| + | <StructureSection load='1yyf' size='340' side='right'caption='[[1yyf]], [[Resolution|resolution]] 4.16Å' scene=''> |
- | |SITE=
| + | == Structural highlights == |
- | |LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene> | + | <table><tr><td colspan='2'>[[1yyf]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] and [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. The August 2006 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''AAA+ Proteases'' by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2006_8 10.2210/rcsb_pdb/mom_2006_8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YYF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YYF FirstGlance]. <br> |
- | |ACTIVITY=
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 4.16Å</td></tr> |
- | |GENE= hslU, htpI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]), hslV, clpQ, codW ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])
| + | <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=1yyf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yyf OCA], [https://pdbe.org/1yyf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yyf RCSB], [https://www.ebi.ac.uk/pdbsum/1yyf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yyf 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/yy/1yyf_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=1yyf ConSurf]. |
| + | <div style="clear:both"></div> |
| | | |
- | '''Correction of X-ray Intensities from an HslV-HslU co-crystal containing lattice translocation defects'''
| + | ==See Also== |
- | | + | *[[Heat Shock Protein structures|Heat Shock Protein structures]] |
- | | + | == References == |
- | ==Overview== | + | <references/> |
- | Because of lattice-translocation defects, two identical but translated lattices can coexist as a single coherent mosaic block in a crystal. The observed structure in such cases is a weighted sum of two identical but translated structures, one from each lattice; the observed structure factors are a weighted vector sum of the structure factors with identical unit amplitudes but shifted phases. The correction of X-ray intensities from a single crystal containing these defects of the hybrid HslV-HslU complex, which consists of Escherichia coli HslU and Bacillus subtilis HslV (also known as CodW), is reported. When intensities are not corrected, a biologically irrelevant complex (with CodW from one lattice and HslU from another) is implied to exist. Only upon correction does a biologically functional CodW-HslU complex structure emerge.
| + | __TOC__ |
- | | + | </StructureSection> |
- | ==About this Structure==
| + | |
- | 1YYF is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] and [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. The following page contains interesting information on the relation of 1YYF with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb80_1.html AAA+ Proteases]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YYF OCA].
| + | |
- | | + | |
- | ==Reference== | + | |
- | Correction of X-ray intensities from an HslV-HslU co-crystal containing lattice-translocation defects., Wang J, Rho SH, Park HH, Eom SH, Acta Crystallogr D Biol Crystallogr. 2005 Jul;61(Pt 7):932-41. Epub 2005, Jun 24. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15983416 15983416]
| + | |
| [[Category: AAA+ Proteases]] | | [[Category: AAA+ Proteases]] |
| [[Category: Bacillus subtilis]] | | [[Category: Bacillus subtilis]] |
| [[Category: Escherichia coli]] | | [[Category: Escherichia coli]] |
- | [[Category: Protein complex]] | + | [[Category: Large Structures]] |
- | [[Category: Eom, S H.]] | + | [[Category: RCSB PDB Molecule of the Month]] |
- | [[Category: Park, H H.]] | + | [[Category: Eom SH]] |
- | [[Category: Rho, S H.]] | + | [[Category: Park HH]] |
- | [[Category: Wang, J.]] | + | [[Category: Rho SH]] |
- | [[Category: ADP]] | + | [[Category: Wang J]] |
- | [[Category: atp-dependent proteolysis]]
| + | |
- | [[Category: hslv-hslu]]
| + | |
- | [[Category: lattice translocation defect]]
| + | |
- | [[Category: quaternary structure]]
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- | | + | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 14:24:54 2008''
| + | |
| Structural highlights
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
- ↑ 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
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