PDBsum entry 3mh7

Hydrolase

PDB id

3mh7

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Contents

			Protein chain

					392 a.a. *

			Ligands

					UNK-UNK-UNK-UNK- UNK ×2

* Residue conservation analysis

PDB id:

3mh7

Links

Name:

Hydrolase

Title:

Htra proteases are activated by a conserved mechanism that can be triggered by distinct molecular cues

Structure:

Protease do. Chain: a. Synonym: degp, htra. Engineered: yes. Mutation: yes. 5-mer peptide. Chain: b, c. Engineered: yes. Other_details: this peptide apparently picked up during protein

Source:

Escherichia coli. Organism_taxid: 83333. Strain: k12. Gene: degp. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.96Å

R-factor:

0.201

R-free:

0.249

Authors:

T.Krojer,J.Sawa,R.Huber,T.Clausen

Key ref:

T.Krojer et al. (2010). HtrA proteases have a conserved activation mechanism that can be triggered by distinct molecular cues. Nat Struct Biol, 17, 844-852. PubMed id: 20581825

Date:

07-Apr-10

Release date:

30-Jun-10

PROCHECK

	Headers

	References

Protein chain

P0C0V0 (DEGP_ECOLI) - Periplasmic serine endoprotease DegP from Escherichia coli (strain K12)

Seq: Struc:					474 a.a. 392 a.a.*

Key:

PfamA domain

Secondary structure

CATH domain

* PDB and UniProt seqs differ at 1 residue position (black cross)



		Enzyme reactions

Enzyme class:

E.C.3.4.21.107 - peptidase Do.

[IntEnz] [ExPASy] [KEGG] [BRENDA]

	Nat Struct Biol 17:844-852 (2010)
PubMed id: 20581825

HtrA proteases have a conserved activation mechanism that can be triggered by distinct molecular cues.
T.Krojer, J.Sawa, R.Huber, T.Clausen.

ABSTRACT

HtrA proteases are tightly regulated proteolytic assemblies that are essential for maintaining protein homeostasis in extracytosolic compartments. Though HtrA proteases have been characterized in detail, their precise molecular mechanism for switching between different functional states is still unknown. To address this, we carried out biochemical and structural studies of DegP from Escherichia coli. We show that effector-peptide binding to the PDZ domain of DegP induces oligomer conversion from resting hexameric DegP6 into proteolytically active 12-mers and 24-mers (DegP12/24). Moreover, our data demonstrate that a specific protease loop (L3) functions as a conserved molecular switch of HtrA proteases. L3 senses the activation signal-that is, the repositioned PDZ domain of substrate-engaged DegP12/24 or the binding of allosteric effectors to regulatory HtrA proteases such as DegS-and transmits this information to the active site. Implications for protein quality control and regulation of oligomeric enzymes are discussed.

Literature references that cite this PDB file's key reference

PubMed id

Reference

22245966

H.Malet, F.Canellas, J.Sawa, J.Yan, K.Thalassinos, M.Ehrmann, T.Clausen, and H.R.Saibil (2012).
Newly folded substrates inside the molecular cage of the HtrA chaperone DegQ.

Nat Struct Mol Biol, 19, 152-157.

PDB codes:

4a8a 4a8b 4a8c 4a8d 4a9g

21532594

J.Kley, B.Schmidt, B.Boyanov, P.C.Stolt-Bergner, R.Kirk, M.Ehrmann, R.R.Knopf, L.Naveh, Z.Adam, and T.Clausen (2011).
Structural adaptation of the plant protease Deg1 to repair photosystem II during light exposure.

Nat Struct Mol Biol, 18, 728-731.

PDB code:

3qo6

21297635

L.Truebestein, A.Tennstaedt, T.Mönig, T.Krojer, F.Canellas, M.Kaiser, T.Clausen, and M.Ehrmann (2011).
Substrate-induced remodeling of the active site regulates human HTRA1 activity.

Nat Struct Mol Biol, 18, 386-388.

PDB codes:

3num 3nwu 3nzi

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.