PDBsum entry 5ji2

Hydrolase

PDB id: 5ji2

Contents

Protein chains

174 a.a.

375 a.a.

353 a.a.

Ligands

ADP ×2

Metals

_MG ×3

PDB id:

5ji2

Name:

Hydrolase

Title:

Hslu l199q in hsluv complex

Structure:

Atp-dependent protease subunit hslv. Chain: a, b, c, d. Synonym: heat shock protein hslv. Engineered: yes. Atp-dependent protease atpase subunit hslu. Chain: e, f. Synonym: heat shock protein hslu,unfoldase hslu. Engineered: yes. Mutation: yes

Source:

Escherichia coli (strain 55989 / eaec). Organism_taxid: 585055. Strain: 55989 / eaec. Gene: hslv, ec55989_4410. Expressed in: escherichia coli. Expression_system_taxid: 562. Escherichia coli o157:h7. Organism_taxid: 83334. Gene: hslu, htpi, z5478, ecs4858.

Resolution:

3.31Å R-factor: 0.239 R-free: 0.281

Authors:

R.A.Grant,R.T.Sauer,K.R.Schmitz,V.Baytshtok

Key ref:

V.Baytshtok et al. (2016). A Structurally Dynamic Region of the HslU Intermediate Domain Controls Protein Degradation and ATP Hydrolysis. Structure, 24, 1766-1777. PubMed id: 27667691

Date:

21-Apr-16 Release date: 30-Nov-16

Protein chains

B7LA29  (HSLV_ECO55) -  ATP-dependent protease subunit HslV from Escherichia coli (strain 55989 / EAEC)

Seq: 176 a.a.

Struc: 174 a.a.

Protein chain

P0A6H6  (HSLU_ECO57) -  ATP-dependent protease ATPase subunit HslU from Escherichia coli O157:H7

Seq: 443 a.a.

Struc: 375 a.a.*

Protein chain

P0A6H6  (HSLU_ECO57) -  ATP-dependent protease ATPase subunit HslU from Escherichia coli O157:H7

Seq: 443 a.a.

Struc: 353 a.a.*

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

Enzyme reactions

• Enzyme class: Chains A, B, C, D: E.C.3.4.25.2 - HslU--HslV peptidase.

Structure 24:1766-1777 (2016)

PubMed id: 27667691

A Structurally Dynamic Region of the HslU Intermediate Domain Controls Protein Degradation and ATP Hydrolysis.

V.Baytshtok, X.Fei, R.A.Grant, T.A.Baker, R.T.Sauer.

ABSTRACT

The I domain of HslU sits above the AAA+ ring and forms a funnel-like entry to the axial pore, where protein substrates are engaged, unfolded, and translocated into HslV for degradation. The L199Q I-domain substitution, which was originally reported as a loss-of-function mutation, resides in a segment that appears to adopt multiple conformations as electron density is not observed in HslU and HslUV crystal structures. The L199Q sequence change does not alter the structure of the AAA+ ring or its interactions with HslV but increases I-domain susceptibility to limited endoproteolysis. Notably, the L199Q mutation increases the rate of ATP hydrolysis substantially, results in slower degradation of some proteins but faster degradation of other substrates, and markedly changes the preference of HslUV for initiating degradation at the N or C terminus of model substrates. Thus, a structurally dynamic region of the I domain plays a key role in controlling protein degradation by HslUV.