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[[Image:1mbu.jpg|left|200px]]


{{Structure
==Crystal Structure Analysis of ClpSN heterodimer==
|PDB= 1mbu |SIZE=350|CAPTION= <scene name='initialview01'>1mbu</scene>, resolution 2.30&Aring;
<StructureSection load='1mbu' size='340' side='right'caption='[[1mbu]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=YBT:BIS-(2-HYDROXYETHYL)AMINO-TRIS(HYDROXYMETHYL)METHANE+YTTRIUM'>YBT</scene>
<table><tr><td colspan='2'>[[1mbu]] is a 4 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=1MBU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MBU 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]] 2.3&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=YBT:BIS-(2-HYDROXYETHYL)AMINO-TRIS(HYDROXYMETHYL)METHANE+YTTRIUM'>YBT</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mbu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mbu OCA], [https://pdbe.org/1mbu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mbu RCSB], [https://www.ebi.ac.uk/pdbsum/1mbu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mbu ProSAT]</span></td></tr>
|RELATEDENTRY=[[1mbv|1MBV]], [[1mbx|1MBX]]
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mbu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mbu OCA], [http://www.ebi.ac.uk/pdbsum/1mbu PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mbu RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/CLPA_ECOLI CLPA_ECOLI] ATP-dependent specificity component of the ClpAP protease. It directs the protease to specific substrates. It has unfoldase activity. The primary function of the ClpA-ClpP complex appears to be the degradation of unfolded or abnormal proteins.
== 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/mb/1mbu_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=1mbu ConSurf].
<div style="clear:both"></div>


'''Crystal Structure Analysis of ClpSN heterodimer'''
==See Also==
 
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
 
__TOC__
==Overview==
</StructureSection>
Substrate selectivity and proteolytic activity for the E. coli ATP-dependent protease, ClpAP, is modulated by an adaptor protein, ClpS. ClpS binds to ClpA, the regulatory component of the ClpAP complex. We report the crystal structure of ClpS in complex with the isolated N-terminal domain of ClpA in two different crystal forms at 2.3- and 3.3-A resolution. The ClpS structure forms an alpha/beta-sandwich and is topologically analogous to the C-terminal domain of the ribosomal protein L7/L12. ClpS contacts two surfaces on the N-terminal domain in both crystal forms; the more extensive interface was shown to be favored in solution by protease protection experiments. The N-terminal 20 residues of ClpS are not visible in the crystal structures; the removal of the first 17 residues produces ClpSDeltaN, which binds to the ClpA N-domain but no longer inhibits ClpA activity. A zinc binding site involving two His and one Glu residue was identified crystallographically in the N-terminal domain of ClpA. In a model of ClpS bound to hexameric ClpA, ClpS is oriented with its N terminus directed toward the distal surface of ClpA, suggesting that the N-terminal region of ClpS may affect productive substrate interactions at the apical surface or substrate entry into the ClpA translocation channel.
 
==About this Structure==
1MBU is a [[Protein complex]] structure of sequences 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=1MBU OCA].
 
==Reference==
Crystal structure of the heterodimeric complex of the adaptor, ClpS, with the N-domain of the AAA+ chaperone, ClpA., Guo F, Esser L, Singh SK, Maurizi MR, Xia D, J Biol Chem. 2002 Nov 29;277(48):46753-62. Epub 2002 Sep 15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12235156 12235156]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Esser, L.]]
[[Category: Esser L]]
[[Category: Guo, F.]]
[[Category: Guo F]]
[[Category: Maurizi, M R.]]
[[Category: Maurizi MR]]
[[Category: Singh, S K.]]
[[Category: Singh SK]]
[[Category: Xia, D.]]
[[Category: Xia D]]
[[Category: protein binding]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:14:06 2008''

Latest revision as of 10:42, 14 February 2024

Crystal Structure Analysis of ClpSN heterodimerCrystal Structure Analysis of ClpSN heterodimer

Structural highlights

1mbu is a 4 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 2.3Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CLPA_ECOLI ATP-dependent specificity component of the ClpAP protease. It directs the protease to specific substrates. It has unfoldase activity. The primary function of the ClpA-ClpP complex appears to be the degradation of unfolded or abnormal proteins.

Evolutionary Conservation

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

See Also

1mbu, resolution 2.30Å

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