PDBsum entry 2k4r

Hydrolase

PDB id

2k4r

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Contents

			Protein chain

					77 a.a. *

* Residue conservation analysis

PDB id:

2k4r

Links
- PDBe
- RCSB
- MMDB
- JenaLib
- Proteopedia
- CATH
- SCOP
- PDBSWS
- ProSAT

Name:

Hydrolase

Title:

Nmr solution structure of the neurotrypsin kringle domain

Structure:

Neurotrypsin. Chain: a. Fragment: kringle domain, nt/k, sequence database residues 84-160. Engineered: yes. Other_details: formula mass: 8533 da (natural abundance), 8635 da (15n-enriched), extinction coefficient (280 nm): 30855 m-1cm-1

Source:

Rattus norvegicus. Rat. Organism_taxid: 10116. Gene: prss12, nt. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

29 models

Authors:

O.A.Ozhogina

Key ref:

O.A.Ozhogina et al. (2008). NMR solution structure of the neurotrypsin Kringle domain. Biochemistry, 47, 12290-12298. PubMed id: 18956887

Date:

16-Jun-08

Release date:

09-Dec-08

PROCHECK

	Headers

	References

Protein chain

G3V801 (NETR_RAT) - Neurotrypsin from Rattus norvegicus

Seq: Struc:

Seq: Struc:					761 a.a. 77 a.a.*

Key:

PfamA domain

Secondary structure

CATH domain

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



		Enzyme reactions

Enzyme class:

E.C.3.4.21.- - ?????

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

	Biochemistry 47:12290-12298 (2008)
PubMed id: 18956887

NMR solution structure of the neurotrypsin Kringle domain.
O.A.Ozhogina, A.Grishaev, E.L.Bominaar, L.Patthy, M.Trexler, M.Llinás.

ABSTRACT

Neurotrypsin is a multidomain protein that serves as a brain-specific serine protease. Here we report the NMR structure of its kringle domain, NT/K. The data analysis was performed with the BACUS (Bayesian analysis of coupled unassigned spins) algorithm. This study presents the first application of BACUS to the structure determination of a 13C unenriched protein for which no prior experimental 3D structure was available. NT/K adopts the kringle fold, consisting of an antiparallel beta-sheet bridged by an overlapping pair of disulfides. The structure reveals the presence of a surface-exposed left-handed polyproline II helix that is closely packed to the core beta-structure. This feature distinguishes NT/K from other members of the kringle fold and points toward a novel functional role for a kringle domain. Functional divergence among kringle domains is discussed on the basis of their surface and electrostatic characteristics.

Literature references that cite this PDB file's key reference

PubMed id

Reference

19524679

O.A.Ozhogina, and E.L.Bominaar (2009).
Characterization of the kringle fold and identification of a ubiquitous new class of disulfide rotamers.

J Struct Biol, 168, 223-233.

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.