PDBsum entry 2m3v

Hydrolase

PDB id: 2m3v

Contents

Protein chain

193 a.a.

PDB id:

2m3v

Name:

Hydrolase

Title:

Solution structure of tyrosine phosphatase related to biofilm formation a (tpba) from pseudomonas aeruginosa

Structure:

Putative uncharacterized protein. Chain: a. Engineered: yes

Source:

Pseudomonas aeruginosa. Organism_taxid: 208963. Strain: ucbpp-pa14. Gene: pa14_13660. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

20 models

Authors:

D.Koveal,W.Peti,R.Page

Key ref:

D.Koveal et al. (2013). Ligand binding reduces conformational flexibility in the active site of tyrosine phosphatase related to biofilm formation A (TpbA) from Pseudomonasaeruginosa. J Mol Biol, 425, 2219-2231. PubMed id: 23524133 DOI: 10.1016/j.jmb.2013.03.023

Date:

26-Jan-13 Release date: 03-Apr-13

Protein chain

A0A0H2ZFK2  (TPBA_PSEAB) -  Dual specificity protein phosphatase TpbA from Pseudomonas aeruginosa (strain UCBPP-PA14)

Seq: 218 a.a.

Struc: 193 a.a.*

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

Enzyme reactions

• Enzyme class 2: E.C.3.1.3.16 - protein-serine/threonine phosphatase.
• Reaction:
  1. O-phospho-L-seryl-[protein] + H2O = L-seryl-[protein] + phosphate
  2. O-phospho-L-threonyl-[protein] + H2O = L-threonyl-[protein] + phosphate
• Enzyme class 3: E.C.3.1.3.48 - protein-tyrosine-phosphatase.
• Reaction: O-phospho-L-tyrosyl-[protein] + H2O = L-tyrosyl-[protein] + phosphate

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.

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1016/j.jmb.2013.03.023

J Mol Biol 425:2219-2231 (2013)

PubMed id: 23524133

Ligand binding reduces conformational flexibility in the active site of tyrosine phosphatase related to biofilm formation A (TpbA) from Pseudomonasaeruginosa.

D.Koveal, M.W.Clarkson, T.K.Wood, R.Page, W.Peti.

ABSTRACT

Tyrosine phosphatase related to biofilm formation A (TpbA) is a periplasmic dual-specificity phosphatase (DUSP) that controls biofilm formation in the pathogenic bacterium Pseudomonas aeruginosa. While DUSPs are known to regulate important cellular functions in both prokaryotes and eukaryotes, very few structures of bacterial DUSPs are available. Here, we present the solution structure of TpbA in the ligand-free open conformation, along with an analysis of the structural and dynamic changes that accompany ligand/phosphate binding. While TpbA adopts a typical DUSP fold, it also possesses distinct structural features that distinguish it from eukaryotic DUSPs. These include additional secondary structural elements, β0 and α6, and unique conformations of the variable insert, the α4-α5 loop and helix α5 that impart TpbA with a flat active-site surface. In the absence of ligand, the protein tyrosine phosphatase loop is disordered and the general acid loop adopts an open conformation, placing the catalytic aspartate, Asp105, more than 11Å away from the active site. Furthermore, the loops surrounding the active site experience motions on multiple timescales, consistent with a combination of conformational heterogeneity and fast (picosecond to nanosecond) timescale dynamics, which are significantly reduced upon ligand binding. Taken together, these data structurally distinguish TpbA and possibly other bacterial DUSPs from eukaryotic DUSPs and provide a rich picture of active-site dynamics in the ligand-free state that are lost upon ligand binding.