PDBsum entry 4a8a

Hydrolase/hydrolase

PDB id: 4a8a

Contents

Protein chains

(+ 6 more) 385 a.a.*

129 a.a.*

* C-alpha coords only

PDB id:

4a8a

Name:

Hydrolase/hydrolase

Title:

Asymmetric cryo-em reconstruction of e. Coli degq 12-mer in complex with lysozyme

Structure:

Periplasmic ph-dependent serine endoprotease degq. Chain: a, b, c, d, e, f, g, h, i, j, k, l. Synonym: protease do, degq. Engineered: yes. Mutation: yes. LysozymE C. Chain: m. Synonym: 1,4-beta-n-acetylmuramidasE C, allergen gal d iv, gal d 4. Ec: 3.2.1.17

Source:

Escherichia coli. Organism_taxid: 83333. Strain: k-12. Tissue: periplasm. Expressed in: escherichia coli. Expression_system_taxid: 469008. Gallus gallus. Chicken. Organism_taxid: 9031.

Authors:

H.Malet,F.Canellas,J.Sawa,J.Yan,K.Thalassinos,M.Ehrmann,T.Clausen, H.R.Saibil

Key ref:

H.Malet et al. (2012). Newly folded substrates inside the molecular cage of the HtrA chaperone DegQ. Nat Struct Biol, 19, 152-157. PubMed id: 22245966

Date:

20-Nov-11 Release date: 28-Dec-11

Protein chains

P39099  (DEGQ_ECOLI) -  Periplasmic pH-dependent serine endoprotease DegQ from Escherichia coli (strain K12)

Seq: 455 a.a.

Struc: 385 a.a.*

Protein chain

P00698  (LYSC_CHICK) -  Lysozyme C from Gallus gallus

Seq: 147 a.a.

Struc: 129 a.a.

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

Enzyme reactions

• Enzyme class 2: Chains A, B, C, D, E, F, G, H, I, J, K, L: E.C.3.4.21.107 - peptidase Do.
• Enzyme class 3: Chain M: E.C.3.2.1.17 - lysozyme.
• Reaction: Hydrolysis of the 1,4-beta-linkages between N-acetyl-D-glucosamine and N-acetylmuramic acid in peptidoglycan heteropolymers of the prokaryotes cell walls.

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

Nat Struct Biol 19:152-157 (2012)

PubMed id: 22245966

Newly folded substrates inside the molecular cage of the HtrA chaperone DegQ.

H.Malet, F.Canellas, J.Sawa, J.Yan, K.Thalassinos, M.Ehrmann, T.Clausen, H.R.Saibil.

ABSTRACT

No abstract given.