PDBsum entry 1ujc

Hydrolase

PDB id

1ujc

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Contents

			Protein chain

					156 a.a. *

			Ligands

					WO4

			Metals

					_CA

			Waters ×234

* Residue conservation analysis

PDB id:

1ujc

Links

Name:

Hydrolase

Title:

Structure of the protein histidine phosphatase sixa complexed with tungstate

Structure:

Phosphohistidine phosphatase sixa. Chain: a. Synonym: protein histidine phosphatase sixa, rx6. Engineered: yes

Source:

Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Resolution:

1.90Å

R-factor:

0.199

R-free:

0.256

Authors:

K.Hamada,M.Kato,T.Shimizu,K.Ihara,T.Mizuno,T.Hakoshima

Key ref:

K.Hamada et al. (2005). Crystal structure of the protein histidine phosphatase SixA in the multistep His-Asp phosphorelay. Genes Cells, 10, 1. PubMed id: 15670209

Date:

31-Jul-03

Release date:

25-Jan-05

PROCHECK

	Headers

	References

Protein chain

P76502 (SIXA_ECOLI) - Phosphohistidine phosphatase SixA from Escherichia coli (strain K12)

Seq: Struc:					161 a.a. 156 a.a.

Key:

PfamA domain

Secondary structure

CATH domain



		Enzyme reactions

Enzyme class:

E.C.3.1.3.- - ?????

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

	Genes Cells 10:1 (2005)
PubMed id: 15670209

Crystal structure of the protein histidine phosphatase SixA in the multistep His-Asp phosphorelay.
K.Hamada, M.Kato, T.Shimizu, K.Ihara, T.Mizuno, T.Hakoshima.

ABSTRACT

The multiple histidine-aspartate phosphorelay system plays a crucial role in cellular adaptation to environments in microorganisms and plants. Like kinase-phosphatase systems in higher eukaryotes, the multiple steps provide additional regulatory checkpoints with phosphatases. The Escherichia coli phosphatase SixA exhibits protein phosphatase activity against the histidine-containing phosphotransfer (HPt) domain located in the C-terminus of the histidine kinase ArcB engaged in anaerobic responses. We have determined the crystal structures of the free and tungstate-bound forms of SixA at 2.06 A and 1.90 A resolution, respectively. The results provide the first three-dimensional view of a bacterial protein histidine phosphatase, revealing a compact alpha/beta architecture related to a family of phosphatases containing the arginine-histidine-glycine (RHG) motif at their active sites. Compared with these RHG phosphatases, SixA lacks an extra alpha-helical subdomain as a lid over the active site, thereby forming a relatively shallow groove important for the accommodation of the HPt domain of ArcB. The tungstate ion, which mimics the substrate phosphate group, is located at the centre of the active site where the active residue, His8, points to the tungsten atom in the mode of in-line nucleophilic attack.

Literature references that cite this PDB file's key reference

PubMed id

Reference

18937503

Y.Chen, J.Jakoncic, J.Wang, X.Zheng, N.Carpino, and N.Nassar (2008).
Structural and functional characterization of the c-terminal domain of the ecdysteroid phosphate phosphatase from bombyx mori reveals a new enzymatic activity.

Biochemistry, 47, 12135-12145.

PDB code:

3c7t

18398008

Z.Lu, D.Dunaway-Mariano, and K.N.Allen (2008).
The catalytic scaffold of the haloalkanoic acid dehalogenase enzyme superfamily acts as a mold for the trigonal bipyramidal transition state.

Proc Natl Acad Sci U S A, 105, 5687-5692.

PDB codes:

2rar 2rav 2rb5 2rbk

17348005

L.Davies, I.P.Anderson, P.C.Turner, A.D.Shirras, H.H.Rees, and D.J.Rigden (2007).
An unsuspected ecdysteroid/steroid phosphatase activity in the key T-cell regulator, Sts-1: surprising relationship to insect ecdysteroid phosphate phosphatase.

Proteins, 67, 720-731.

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. Where a reference describes a PDB structure, the PDB code is shown on the right.