PDBsum entry 3gq7

Viral protein

PDB id

3gq7

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Contents

			Protein chain

					605 a.a. *

			Ligands

					PO4


					CO3

			Metals

					_CA


					_MG

			Waters ×439

* Residue conservation analysis

PDB id:

3gq7

Links

Name:

Viral protein

Title:

Crystal structure of the bacteriophage phi29 gene product 12 n- terminal fragment

Structure:

Preneck appendage protein. Chain: a. Fragment: d1 D2d3, residues 89-691. Engineered: yes

Source:

Bacillus phage phi29. Organism_taxid: 10756. Gene: 12, gene product 12. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.05Å

R-factor:

0.159

R-free:

0.190

Authors:

Y.Xiang,M.G.Rossmann

Key ref:

Y.Xiang et al. (2009). Crystallographic insights into the autocatalytic assembly mechanism of a bacteriophage tail spike. Mol Cell, 34, 375-386. PubMed id: 19450535

Date:

24-Mar-09

Release date:

26-May-09

PROCHECK

	Headers

	References

Protein chain

P20345 (FIB12_BPPH2) - Pre-neck appendage protein from Bacillus phage phi29

Seq: Struc:

Seq: Struc:					854 a.a. 605 a.a.*

Key:

PfamA domain

Secondary structure

CATH domain

* PDB and UniProt seqs differ at 8 residue positions (black crosses)



		Enzyme reactions

Enzyme class:

E.C.?

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

	Mol Cell 34:375-386 (2009)
PubMed id: 19450535

Crystallographic insights into the autocatalytic assembly mechanism of a bacteriophage tail spike.
Y.Xiang, P.G.Leiman, L.Li, S.Grimes, D.L.Anderson, M.G.Rossmann.

ABSTRACT

The tailed bacteriophage phi29 has 12 "appendages" (gene product 12, gp12) attached to its neck region that participate in host cell recognition and entry. In the cell, monomeric gp12 undergoes proteolytic processing that releases the C-terminal domain during assembly into trimers. We report here crystal structures of the protein before and after catalytic processing and show that the C-terminal domain of gp12 is an "autochaperone" that aids trimerization. We also show that autocleavage of the C-terminal domain is a posttrimerization event that is followed by a unique ATP-dependent release. The posttranslationally modified N-terminal part has three domains that function to attach the appendages to the phage, digest the cell wall teichoic acids, and bind irreversibly to the host, respectively. Structural and sequence comparisons suggest that some eukaryotic and bacterial viruses as well as bacterial adhesins might have a similar maturation mechanism as is performed by phi29 gp12 for Bacillus subtilis.

Literature references that cite this PDB file's key reference

PubMed id

Reference

20118935

E.C.Schulz, A.Dickmanns, H.Urlaub, A.Schmitt, M.Mühlenhoff, K.Stummeyer, D.Schwarzer, R.Gerardy-Schahn, and R.Ficner (2010).
Crystal structure of an intramolecular chaperone mediating triple-beta-helix folding.

Nat Struct Mol Biol, 17, 210-215.

PDB codes:

3gud 3gw6

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.