PDBsum entry 3ju4

Hydrolase

PDB id

3ju4

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Contents

			Protein chain

					670 a.a. *

			Ligands

					SLB

			Metals

					_NA


					_CL ×5

			Waters ×1616

* Residue conservation analysis

PDB id:

3ju4

Links

Name:

Hydrolase

Title:

Crystal structure analysis of endosialidasenf at 0.98 a resolution

Structure:

Endo-n-acetylneuraminidase. Chain: a. Fragment: unp residues 246-910. Synonym: endonf, endo-n, endosialidase, g102. Engineered: yes

Source:

Enterobacteria phage k1f. Bacteriophage k1f. Organism_taxid: 344021. Strain: k1. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

0.98Å

R-factor:

0.116

R-free:

0.133

Authors:

E.C.Schulz,P.Neuman,R.Gerardy-Schahn,G.M.Sheldrick,R.Ficner

Key ref:

E.C.Schulz et al. (2010). Structure analysis of endosialidase NF at 0.98 A resolution. Acta Crystallogr D Biol Crystallogr, 66, 176-180. PubMed id: 20124697

Date:

14-Sep-09

Release date:

02-Feb-10

PROCHECK

	Headers

	References

Protein chain

Q04830 (FIBER_BPK1F) - Tail spike protein from Escherichia phage K1F

Seq: Struc:

Seq: Struc:

Seq: Struc:					1064 a.a. 670 a.a.*

Key:

PfamA domain

Secondary structure

CATH domain

* PDB and UniProt seqs differ at 3 residue positions (black crosses)



		Enzyme reactions

Enzyme class:

E.C.3.2.1.129 - endo-alpha-sialidase.

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

Reaction:

Endohydrolysis of (2->8)-alpha-sialosyl linkages in oligo- or poly(sialic) acids.

	Acta Crystallogr D Biol Crystallogr 66:176-180 (2010)
PubMed id: 20124697

Structure analysis of endosialidase NF at 0.98 A resolution.
E.C.Schulz, P.Neumann, R.Gerardy-Schahn, G.M.Sheldrick, R.Ficner.

ABSTRACT

Endosialidase NF (endoNF) is a bacteriophage-derived endosialidase that specifically degrades alpha-2,8-linked polysialic acid. The structure of a new crystal form of endoNF in complex with sialic acid has been refined at 0.98 A resolution. The 210 kDa homotrimeric multi-domain enzyme displays outstanding stability and resistance to SDS. Even at atomic resolution, only a minor fraction of side chains possess alternative conformations. However, multiple conformations of an active-site residue imply that it has an important catalytic function in the cleavage mechanism of polysialic acid.