PDBsum entry 2zrq

Hydrolase

PDB id

2zrq

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Contents

			Protein chain

					318 a.a. *

			Metals

					_CA ×7

			Waters ×188

* Residue conservation analysis

PDB id:

2zrq

Links
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Name:

Hydrolase

Title:

Crystal structure of s324a-subtilisin

Structure:

Tk-subtilisin. Chain: a. Fragment: unp residues 94-422. Engineered: yes. Mutation: yes

Source:

Pyrococcus kodakaraensis. Thermococcus kodakaraensis. Organism_taxid: 69014. Gene: tk1675. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

2.16Å

R-factor:

0.147

R-free:

0.197

Authors:

S.Tanaka,Y.Takeuchi,H.Matsumura,Y.Koga,K.Takano,S.Kanaya

Key ref:

S.Tanaka et al. (2008). Crystal structure of Tk-subtilisin folded without propeptide: requirement of propeptide for acceleration of folding. Febs Lett, 582, 3875-3878. PubMed id: 18951896

Date:

28-Aug-08

Release date:

03-Mar-09

PROCHECK

	Headers

	References

Protein chain

P58502 (TKSU_THEKO) - Tk-subtilisin from Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)

Seq: Struc:					422 a.a. 318 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]

	Febs Lett 582:3875-3878 (2008)
PubMed id: 18951896

Crystal structure of Tk-subtilisin folded without propeptide: requirement of propeptide for acceleration of folding.
S.Tanaka, Y.Takeuchi, H.Matsumura, Y.Koga, K.Takano, S.Kanaya.

ABSTRACT

Tk-subtilisin (a subtilisin homologue from Thermococcus kodakaraensis) is matured from Pro-Tk-subtilisin upon autoprocessing and degradation of Tk-propeptide. To analyze the folding mechanism of Tk-subtilisin, the crystal structure of the active site mutant of Tk-subtilisin (S324A-subtilisin*), which was refolded in the presence of Ca2+ and absence of Tk-propeptide, was determined at 2.16A resolution. This structure is essentially the same as that of Tk-subtilisin matured from Pro-Tk-subtilisin. S324A-subtilisin* was refolded with a rate constant of 0.17 and 1.8min(-1) at 30 degrees C in the absence and presence of Tk-propeptide, respectively, indicating that Tk-subtilisin does not require Tk-propeptide for folding but requires it for acceleration of folding.

Literature references that cite this PDB file's key reference

PubMed id

Reference

20100702

T.Foophow, S.Tanaka, Y.Koga, K.Takano, and S.Kanaya (2010).
Subtilisin-like serine protease from hyperthermophilic archaeon Thermococcus kodakaraensis with N- and C-terminal propeptides.

Protein Eng Des Sel, 23, 347-355.

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.