1tyf: Difference between revisions

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[[Image:1tyf.png|left|200px]]


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==THE STRUCTURE OF CLPP AT 2.3 ANGSTROM RESOLUTION SUGGESTS A MODEL FOR ATP-DEPENDENT PROTEOLYSIS==
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<StructureSection load='1tyf' size='340' side='right'caption='[[1tyf]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1tyf]] is a 14 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=1TYF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TYF FirstGlance]. <br>
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</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>
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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=1tyf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tyf OCA], [https://pdbe.org/1tyf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tyf RCSB], [https://www.ebi.ac.uk/pdbsum/1tyf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tyf ProSAT]</span></td></tr>
{{STRUCTURE_1tyf|  PDB=1tyf  |  SCENE=  }}
</table>
 
== Function ==
===THE STRUCTURE OF CLPP AT 2.3 ANGSTROM RESOLUTION SUGGESTS A MODEL FOR ATP-DEPENDENT PROTEOLYSIS===
[https://www.uniprot.org/uniprot/CLPP_ECOLI CLPP_ECOLI] Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. May play the role of a master protease which is attracted to different substrates by different specificity factors such as ClpA or ClpX.
 
== Evolutionary Conservation ==
 
[[Image:Consurf_key_small.gif|200px|right]]
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==About this Structure==
</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=1tyf ConSurf].
[[1tyf]] is a 14 chain structure with 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=1TYF OCA].  
<div style="clear:both"></div>


==See Also==
==See Also==
*[[Clp protease|Clp protease]]
*[[Clp Protease|Clp Protease]]
 
*[[Clp protease 3D structures|Clp protease 3D structures]]
==Reference==
__TOC__
<ref group="xtra">PMID:009390554</ref><references group="xtra"/>
</StructureSection>
[[Category: Endopeptidase Clp]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Flanagan, J M.]]
[[Category: Large Structures]]
[[Category: Hartling, J A.]]
[[Category: Flanagan JM]]
[[Category: Wang, J.]]
[[Category: Hartling JA]]
[[Category: Peptidase]]
[[Category: Wang J]]

Latest revision as of 11:42, 14 February 2024

THE STRUCTURE OF CLPP AT 2.3 ANGSTROM RESOLUTION SUGGESTS A MODEL FOR ATP-DEPENDENT PROTEOLYSISTHE STRUCTURE OF CLPP AT 2.3 ANGSTROM RESOLUTION SUGGESTS A MODEL FOR ATP-DEPENDENT PROTEOLYSIS

Structural highlights

1tyf is a 14 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
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CLPP_ECOLI Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. May play the role of a master protease which is attracted to different substrates by different specificity factors such as ClpA or ClpX.

Evolutionary Conservation

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

See Also

1tyf, resolution 2.30Å

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