1k6k

From Proteopedia

(Difference between revisions)

Revision as of 06:49, 11 August 2021

Crystal Structure of ClpA, an AAA+ Chaperone-like Regulator of ClpAP protease implication to the functional difference of two ATPase domains

Structural highlights

1k6k is a 1 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1ksf
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.

Publication Abstract from PubMed

Escherichia coli ClpA, an Hsp100/Clp chaperone and an integral component of the ATP-dependent ClpAP protease, participates in regulatory protein degradation and the dissolution and degradation of protein aggregates. The crystal structure of the ClpA subunit reveals an N-terminal domain with pseudo-twofold symmetry and two AAA(+) modules (D1 and D2) each consisting of a large and a small sub-domain with ADP bound in the sub-domain junction. The N-terminal domain interacts with the D1 domain in a manner similar to adaptor-binding domains of other AAA(+) proteins. D1 and D2 are connected head-to-tail consistent with a cooperative and vectorial translocation of protein substrates. In a planar hexamer model of ClpA, built by assembling ClpA D1 and D2 into homohexameric rings of known structures of AAA(+) modules, the differences in D1-D1 and D2-D2 interfaces correlate with their respective contributions to hexamer stability and ATPase activity.

Crystal structure of ClpA, an Hsp100 chaperone and regulator of ClpAP protease.,Guo F, Maurizi MR, Esser L, Xia D J Biol Chem. 2002 Nov 29;277(48):46743-52. Epub 2002 Aug 29. PMID:12205096^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Guo F, Maurizi MR, Esser L, Xia D. Crystal structure of ClpA, an Hsp100 chaperone and regulator of ClpAP protease. J Biol Chem. 2002 Nov 29;277(48):46743-52. Epub 2002 Aug 29. PMID:12205096 doi:10.1074/jbc.M207796200

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1k6k"

@@ Line 3: / Line 3: @@
 <StructureSection load='1k6k' size='340' side='right'caption='[[1k6k]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1k6k]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K6K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1K6K FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1k6k]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K6K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K6K FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ksf|1ksf]]</td></tr>
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ksf|1ksf]]</div></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1k6k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k6k OCA], [http://pdbe.org/1k6k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1k6k RCSB], [http://www.ebi.ac.uk/pdbsum/1k6k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1k6k ProSAT]</span></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=1k6k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k6k OCA], [https://pdbe.org/1k6k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k6k RCSB], [https://www.ebi.ac.uk/pdbsum/1k6k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k6k ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://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.
+[[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]]

1k6k

From Proteopedia

Revision as of 06:49, 11 August 2021

Crystal Structure of ClpA, an AAA+ Chaperone-like Regulator of ClpAP protease implication to the functional difference of two ATPase domains

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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