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3dnj

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Revision as of 20:37, 24 December 2014

The structure of the Caulobacter crescentus ClpS protease adaptor protein in complex with a N-end rule peptide

Structural highlights

3dnj is a 4 chain structure with sequence from Caulobacter vibrioides. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:	clpS, CC_2467 (Caulobacter vibrioides)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[CLPS_CAUCR] Involved in the modulation of the specificity of the ClpAP-mediated ATP-dependent protein degradation (By similarity).

Publication Abstract from PubMed

The N-end rule targets specific proteins for destruction in prokaryotes and eukaryotes. Here, we report a crystal structure of a bacterial N-end rule adaptor, ClpS, bound to a peptide mimic of an N-end rule substrate. This structure, which was solved at a resolution of 1.15 A, reveals specific recognition of the peptide alpha-amino group via hydrogen bonding and shows that the peptide's N-terminal tyrosine side chain is buried in a deep hydrophobic cleft that pre-exists on the surface of ClpS. The adaptor side chains that contact the peptide's N-terminal residue are highly conserved in orthologs and in E3 ubiquitin ligases that mediate eukaryotic N-end rule recognition. We show that mutation of critical ClpS contact residues abrogates substrate delivery to and degradation by the AAA+ protease ClpAP, demonstrate that modification of the hydrophobic pocket results in altered N-end rule specificity, and discuss functional implications for the mechanism of substrate delivery.

The molecular basis of N-end rule recognition.,Wang KH, Roman-Hernandez G, Grant RA, Sauer RT, Baker TA Mol Cell. 2008 Nov 7;32(3):406-14. PMID:18995838^[1]

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

References

↑ Wang KH, Roman-Hernandez G, Grant RA, Sauer RT, Baker TA. The molecular basis of N-end rule recognition. Mol Cell. 2008 Nov 7;32(3):406-14. PMID:18995838 doi:http://dx.doi.org/S1097-2765(08)00692-8

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3dnj"

@@ Line 7: / Line 7: @@
 <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=3dnj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dnj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3dnj RCSB], [http://www.ebi.ac.uk/pdbsum/3dnj PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/CLPS_CAUCR CLPS_CAUCR]] Involved in the modulation of the specificity of the ClpAP-mediated ATP-dependent protein degradation (By similarity).
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

3dnj

From Proteopedia

Revision as of 20:37, 24 December 2014

The structure of the Caulobacter crescentus ClpS protease adaptor protein in complex with a N-end rule peptide

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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