PDBsum entry 2x3h

Lyase

PDB id

2x3h

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Contents

			Protein chains

					498 a.a.

			Metals

					_BR ×12

			Waters ×874

PDB id:

2x3h

Links

Name:

Lyase

Title:

Coliphage k5a lyase

Structure:

K5 lyase. Chain: a, b, c. Fragment: residues 1-505. Synonym: k5a lyase. Engineered: yes

Source:

Enterobacteria phage k1-5. Organism_taxid: 187764. Strain: coliphage k5a. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.60Å

R-factor:

0.178

R-free:

0.203

Authors:

J.E.Thompson,M.Pourhossein,M.Goldrick,T.Hudson,J.P.Derrick, I.S.Roberts

Key ref:

J.E.Thompson et al. (2010). The K5 lyase KflA combines a viral tail spike structure with a bacterial polysaccharide lyase mechanism. J Biol Chem, 285, 23963-23969. PubMed id: 20519506

Date:

04-Feb-10

Release date:

02-Jun-10

PROCHECK

	Headers

	References

Protein chains

O09496 (FIBER_BPK5) - Tail spike protein from Escherichia virus K5

Seq: Struc:

Seq: Struc:					632 a.a. 498 a.a.

Key:

PfamA domain

Secondary structure

CATH domain



		Enzyme reactions

Enzyme class:

E.C.4.-.-.-

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

	J Biol Chem 285:23963-23969 (2010)
PubMed id: 20519506

The K5 lyase KflA combines a viral tail spike structure with a bacterial polysaccharide lyase mechanism.
J.E.Thompson, M.Pourhossein, A.Waterhouse, T.Hudson, M.Goldrick, J.P.Derrick, I.S.Roberts.

ABSTRACT

K5 lyase A (KflA) is a tail spike protein (TSP) encoded by K5A coliphage which cleaves K5 capsular polysaccharide, a glycosaminoglycan (GAG) with the repeat unit [-4)-betaGlcA-(1,4)-alphaGlcNAc(1-], displayed on the surface of Escherichia coli K5 strains. The crystal structure of KflA reveals a trimeric arrangement, with each monomer containing a right-handed, single-stranded parallel beta-helix domain. Stable trimer formation by the intertwining of strands in the C-terminal domain, followed by proteolytic maturation, is likely to be catalysed by an autochaperone as described for K1F endosialidase. The structure of KflA represents the first bacteriophage tail spike protein combining polysaccharide lyase activity with a single-stranded parallel beta-helix fold. We propose a catalytic site and mechanism representing convergence with the syn-beta-elimination site of heparinase II from Pedobacter heparinus.

Literature references that cite this PDB file's key reference

PubMed id

Reference

21330133

E.C.Schulz, and R.Ficner (2011).
Knitting and snipping: chaperones in β-helix folding.

Curr Opin Struct Biol, 21, 232-239.

20805221

M.L.Garron, and M.Cygler (2010).
Structural and mechanistic classification of uronic acid-containing polysaccharide lyases.

Glycobiology, 20, 1547-1573.

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.