1r6q
From Proteopedia
(New page: 200px<br /><applet load="1r6q" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r6q, resolution 2.35Å" /> '''ClpNS with fragments...) |
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| - | [[Image:1r6q.gif|left|200px]]<br /><applet load="1r6q" size=" | + | [[Image:1r6q.gif|left|200px]]<br /><applet load="1r6q" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1r6q, resolution 2.35Å" /> | caption="1r6q, resolution 2.35Å" /> | ||
'''ClpNS with fragments'''<br /> | '''ClpNS with fragments'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Escherichia coli ClpA, an Hsp100/Clp chaperone and an integral component | + | Escherichia coli ClpA, an Hsp100/Clp chaperone and an integral component of the ATP-dependent ClpAP protease, participates in the dissolution and degradation of regulatory proteins and protein aggregates. ClpA consists of three functional domains: an N-terminal domain and two ATPase domains, D1 and D2. The N-domain is attached to D1 by a mobile linker and is made up of two tightly bound, identically folded alpha-helical bundles related by a pseudo 2-fold symmetry. Between the halves of the pseudo-dimer is a large flexible acidic loop that becomes better ordered upon binding of the small adaptor protein, ClpS. We have identified a number of structural features in the N-domain, including a Zn(++) binding motif, several interfaces for binding to ClpS, and a prominent hydrophobic surface area that binds peptides in different configurations. These structural motifs may contribute to binding of protein or peptide substrates with weak affinity and broad specificity. Kinetic studies comparing wild-type ClpA to a mutant ClpA with its N-domain deleted show that the N-domains contribute to the binding of a non-specific protein substrate but not of a folded substrate with the specific SsrA recognition tag. A functional model is proposed in which the N-domains in ClpA function as tentacles to weakly hold on to proteins thereby enhancing local substrate concentration. |
==About this Structure== | ==About this Structure== | ||
| - | 1R6Q 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 Y1, YBT and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1R6Q 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=Y1:'>Y1</scene>, <scene name='pdbligand=YBT:'>YBT</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R6Q OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Esser, L.]] | [[Category: Esser, L.]] | ||
[[Category: Guo, F.]] | [[Category: Guo, F.]] | ||
| - | [[Category: Maurizi, M | + | [[Category: Maurizi, M R.]] |
| - | [[Category: Singh, S | + | [[Category: Singh, S K.]] |
[[Category: Xia, D.]] | [[Category: Xia, D.]] | ||
[[Category: GOL]] | [[Category: GOL]] | ||
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[[Category: n-terminal domain]] | [[Category: n-terminal domain]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:47:39 2008'' |
Revision as of 12:47, 21 February 2008
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ClpNS with fragments
Overview
Escherichia coli ClpA, an Hsp100/Clp chaperone and an integral component of the ATP-dependent ClpAP protease, participates in the dissolution and degradation of regulatory proteins and protein aggregates. ClpA consists of three functional domains: an N-terminal domain and two ATPase domains, D1 and D2. The N-domain is attached to D1 by a mobile linker and is made up of two tightly bound, identically folded alpha-helical bundles related by a pseudo 2-fold symmetry. Between the halves of the pseudo-dimer is a large flexible acidic loop that becomes better ordered upon binding of the small adaptor protein, ClpS. We have identified a number of structural features in the N-domain, including a Zn(++) binding motif, several interfaces for binding to ClpS, and a prominent hydrophobic surface area that binds peptides in different configurations. These structural motifs may contribute to binding of protein or peptide substrates with weak affinity and broad specificity. Kinetic studies comparing wild-type ClpA to a mutant ClpA with its N-domain deleted show that the N-domains contribute to the binding of a non-specific protein substrate but not of a folded substrate with the specific SsrA recognition tag. A functional model is proposed in which the N-domains in ClpA function as tentacles to weakly hold on to proteins thereby enhancing local substrate concentration.
About this Structure
1R6Q is a Protein complex structure of sequences from Escherichia coli with , and as ligands. Full crystallographic information is available from OCA.
Reference
Crystallographic investigation of peptide binding sites in the N-domain of the ClpA chaperone., Xia D, Esser L, Singh SK, Guo F, Maurizi MR, J Struct Biol. 2004 Apr-May;146(1-2):166-79. PMID:15037248
Page seeded by OCA on Thu Feb 21 14:47:39 2008
Categories: Escherichia coli | Protein complex | Esser, L. | Guo, F. | Maurizi, M R. | Singh, S K. | Xia, D. | GOL | Y1 | YBT | Aaa+ | Binding mechanism | Clpa | Clps | Crystal | N-terminal domain
