PDBsum entry 3sk9

Hydrolase

PDB id

3sk9

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Contents

			Protein chain

					230 a.a.

			Waters ×105

PDB id:

3sk9

Links

Name:

Hydrolase

Title:

Crystal structure of the thermus thermophilus cas3 hd domain

Structure:

Putative uncharacterized protein tthb187. Chain: a. Engineered: yes

Source:

Thermus thermophilus hb8. Organism_taxid: 300852. Strain: hb8. Gene: tthb187. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.80Å

R-factor:

0.168

R-free:

0.195

Authors:

S.Bailey,S.Mulepati

Key ref:

S.Mulepati and S.Bailey (2011). Structural and biochemical analysis of nuclease domain of clustered regularly interspaced short palindromic repeat (CRISPR)-associated protein 3 (Cas3). J Biol Chem, 286, 31896-31903. PubMed id: 21775431

Date:

22-Jun-11

Release date:

20-Jul-11

PROCHECK

	Headers

	References

Protein chain

Q53VY2 (CAS3_THET8) - CRISPR-associated endonuclease/helicase Cas3 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)

Seq: Struc:

Seq: Struc:					920 a.a. 230 a.a.*

Key:

PfamA domain

Secondary structure

CATH domain

* PDB and UniProt seqs differ at 2 residue positions (black crosses)



		Enzyme reactions

Enzyme class 1:

E.C.3.1.-.-

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

Enzyme class 2:

E.C.3.6.4.- - ?????

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

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

	J Biol Chem 286:31896-31903 (2011)
PubMed id: 21775431

Structural and biochemical analysis of nuclease domain of clustered regularly interspaced short palindromic repeat (CRISPR)-associated protein 3 (Cas3).
S.Mulepati, S.Bailey.

ABSTRACT

No abstract given.

Literature references that cite this PDB file's key reference

PubMed id

Reference

22337052

B.Wiedenheft, S.H.Sternberg, and J.A.Doudna (2012).
RNA-guided genetic silencing systems in bacteria and archaea.

Nature, 482, 331-338.

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.