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PDBsum entry 8xn4
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(+ 1 more)
182 a.a.
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(+ 1 more)
176 a.a.
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PDB id:
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Hydrolase
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Title:
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Cryo-em structure of the clpp degradation system in streptomyces hawaiiensis
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Structure:
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Atp-dependent clp protease proteolytic subunit. Chain: a, b, c, d, e, f, g. Synonym: endopeptidase clp. Engineered: yes. Mutation: yes. Atp-dependent clp protease proteolytic subunit. Chain: h, i, j, k, l, m, n. Synonym: endopeptidase clp. Engineered: yes.
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Source:
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Streptomyces hawaiiensis. Organism_taxid: 67305. Gene: clpp1, clpp, ceb94_14110. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Gene: clpp2, clpp, ceb94_14105. Expression_system_taxid: 469008
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Authors:
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X.Xu,F.Long
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Key ref:
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X.Xu
et al.
Structural insights into the clp protein degradation machinery..
Mbio,
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PubMed id:
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Date:
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29-Dec-23
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Release date:
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27-Mar-24
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PROCHECK
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Headers
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References
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Enzyme class:
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Chains A, B, C, D, E, F, G, H, I, J, K, L, M, N:
E.C.3.4.21.92
- endopeptidase Clp.
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Reaction:
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Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. Alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are cleaved (such as succinyl-Leu-Tyr-|-NHMEC; and Leu-Tyr-Leu-|-Tyr-Trp, in which the cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp- bond also occurs).
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');
}
}
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