1mg9
From Proteopedia
(New page: 200px<br /><applet load="1mg9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mg9, resolution 2.30Å" /> '''The structural basis...) |
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| - | [[Image:1mg9.jpg|left|200px]]<br /><applet load="1mg9" size=" | + | [[Image:1mg9.jpg|left|200px]]<br /><applet load="1mg9" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1mg9, resolution 2.30Å" /> | caption="1mg9, resolution 2.30Å" /> | ||
'''The structural basis of ClpS-mediated switch in ClpA substrate recognition'''<br /> | '''The structural basis of ClpS-mediated switch in ClpA substrate recognition'''<br /> | ||
==Overview== | ==Overview== | ||
| - | In Escherichia coli, protein degradation is performed by several | + | In Escherichia coli, protein degradation is performed by several proteolytic machines, including ClpAP. Generally, the substrate specificity of these machines is determined by chaperone components, such as ClpA. In some cases, however, the specificity is modified by adaptor proteins, such as ClpS. Here we report the 2.5 A resolution crystal structure of ClpS in complex with the N-terminal domain of ClpA. Using mutagenesis, we demonstrate that two contact residues (Glu79 and Lys 84) are essential not only for ClpAS complex formation but also for ClpAPS-mediated substrate degradation. The corresponding residues are absent in the chaperone ClpB, providing a structural rationale for the unique specificity shown by ClpS despite the high overall similarity between ClpA and ClpB. To determine the location of ClpS within the ClpA hexamer, we modeled the N-terminal domain of ClpA onto a structurally defined, homologous AAA+ protein. From this model, we proposed a molecular mechanism to explain the ClpS-mediated switch in ClpA substrate specificity. |
==About this Structure== | ==About this Structure== | ||
| - | 1MG9 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with SPK as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1MG9 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=SPK:'>SPK</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MG9 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bukau, B.]] | [[Category: Bukau, B.]] | ||
[[Category: Cusack, S.]] | [[Category: Cusack, S.]] | ||
| - | [[Category: Dougan, D | + | [[Category: Dougan, D A.]] |
[[Category: Paal, K.]] | [[Category: Paal, K.]] | ||
| - | [[Category: Ravelli, R | + | [[Category: Ravelli, R B.]] |
[[Category: Zeth, K.]] | [[Category: Zeth, K.]] | ||
[[Category: SPK]] | [[Category: SPK]] | ||
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[[Category: substrate sensor]] | [[Category: substrate sensor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:54:58 2008'' |
Revision as of 11:54, 21 February 2008
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The structural basis of ClpS-mediated switch in ClpA substrate recognition
Overview
In Escherichia coli, protein degradation is performed by several proteolytic machines, including ClpAP. Generally, the substrate specificity of these machines is determined by chaperone components, such as ClpA. In some cases, however, the specificity is modified by adaptor proteins, such as ClpS. Here we report the 2.5 A resolution crystal structure of ClpS in complex with the N-terminal domain of ClpA. Using mutagenesis, we demonstrate that two contact residues (Glu79 and Lys 84) are essential not only for ClpAS complex formation but also for ClpAPS-mediated substrate degradation. The corresponding residues are absent in the chaperone ClpB, providing a structural rationale for the unique specificity shown by ClpS despite the high overall similarity between ClpA and ClpB. To determine the location of ClpS within the ClpA hexamer, we modeled the N-terminal domain of ClpA onto a structurally defined, homologous AAA+ protein. From this model, we proposed a molecular mechanism to explain the ClpS-mediated switch in ClpA substrate specificity.
About this Structure
1MG9 is a Protein complex structure of sequences from Escherichia coli with as ligand. Full crystallographic information is available from OCA.
Reference
Structural analysis of the adaptor protein ClpS in complex with the N-terminal domain of ClpA., Zeth K, Ravelli RB, Paal K, Cusack S, Bukau B, Dougan DA, Nat Struct Biol. 2002 Dec;9(12):906-11. PMID:12426582
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