PDBsum entry 3otp

Hydrolase

PDB id

3otp

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Contents

			Protein chains

					(+ 0 more) 381 a.a. *


					16 a.a. *

			Ligands

					TRP-VAL-SER-ALA- ALA ×5


					GLY-ILE-LEU-GLN- ILE ×5

* Residue conservation analysis

PDB id:

3otp

Links

Name:

Hydrolase

Title:

Crystal structure of the degp dodecamer with a model substrate

Structure:

Protease do. Chain: a, b, c, d, e, f. Fragment: unp residues 27-474. Engineered: yes. Mutation: yes. LysozymE C. Chain: g, h, i, j, k, l. Fragment: a model peptide substrate. Engineered: yes.

Source:

Escherichia coli. Organism_taxid: 562. Gene: b0161, degp, htra, jw0157, ptd. Expressed in: escherichia coli. Expression_system_taxid: 562. Gallus gallus. Chicken. Organism_taxid: 9031. Gene: lysozymE C, lyz.

Resolution:

3.76Å

R-factor:

0.220

R-free:

0.251

Authors:

S.Kim,R.A.Grant,R.T.Sauer

Key ref:

S.Kim et al. (2011). Covalent linkage of distinct substrate degrons controls assembly and disassembly of DegP proteolytic cages. Cell, 145, 67-78. PubMed id: 21458668

Date:

13-Sep-10

Release date:

19-Jan-11

PROCHECK

	Headers

	References

Protein chains

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

Seq: Struc:					474 a.a. 381 a.a.*

Protein chain

P00698 (LYSC_CHICK) - Lysozyme C from Gallus gallus

Seq: Struc:					147 a.a. 16 a.a.*

Key:

PfamA domain

Secondary structure

CATH domain

* PDB and UniProt seqs differ at 6 residue positions (black crosses)



		Enzyme reactions

Enzyme class 2:

Chains A, B, C, D, E, F: E.C.3.4.21.107 - peptidase Do.

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

Enzyme class 3:

Chain I: E.C.3.2.1.17 - lysozyme.

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

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.

	Cell 145:67-78 (2011)
PubMed id: 21458668

Covalent linkage of distinct substrate degrons controls assembly and disassembly of DegP proteolytic cages.
S.Kim, R.A.Grant, R.T.Sauer.

ABSTRACT

No abstract given.

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

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.