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PDBsum entry 1u2q

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protein ligands metals links
Hydrolase PDB id
1u2q
Jmol
Contents
Protein chain
155 a.a. *
Ligands
GOL
Metals
_CL
Waters ×83
* Residue conservation analysis
PDB id:
1u2q
Name: Hydrolase
Title: Crystal structure of mycobacterium tuberculosis low molecula protein tyrosine phosphatase (mptpa) at 2.5a resolution wit in the active site
Structure: Low molecular weight protein-tyrosine-phosphatase chain: a. Synonym: ptpase. Engineered: yes
Source: Mycobacterium tuberculosis. Organism_taxid: 1773. Gene: mptpa. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.50Å     R-factor:   0.212     R-free:   0.273
Authors: C.Madhurantakam,E.Rajakumara,P.A.Mazumdar,B.Saha,D.Mitra,H.G R.Sankaranarayanan,A.K.Das
Key ref: C.Madhurantakam et al. (2005). Crystal structure of low-molecular-weight protein tyrosine phosphatase from Mycobacterium tuberculosis at 1.9-A resolution. J Bacteriol, 187, 2175-2181. PubMed id: 15743966
Date:
20-Jul-04     Release date:   22-Mar-05    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam  
P9WIA1  (PTPA_MYCTU) -  Probable low molecular weight protein-tyrosine-phosphatase
Seq:
Struc:
163 a.a.
155 a.a.
Key:    Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.1.3.48  - Protein-tyrosine-phosphatase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Protein tyrosine phosphate + H2O = protein tyrosine + phosphate
Protein tyrosine phosphate
+ H(2)O
= protein tyrosine
+ phosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     host cell endosome   3 terms 
  Biological process     peptidyl-tyrosine dephosphorylation   3 terms 
  Biochemical function     hydrolase activity     3 terms  

 

 
    reference    
 
 
J Bacteriol 187:2175-2181 (2005)
PubMed id: 15743966  
 
 
Crystal structure of low-molecular-weight protein tyrosine phosphatase from Mycobacterium tuberculosis at 1.9-A resolution.
C.Madhurantakam, E.Rajakumara, P.A.Mazumdar, B.Saha, D.Mitra, H.G.Wiker, R.Sankaranarayanan, A.K.Das.
 
  ABSTRACT  
 
The low-molecular-weight protein tyrosine phosphatase (LMWPTPase) belongs to a distinctive class of phosphotyrosine phosphatases widely distributed among prokaryotes and eukaryotes. We report here the crystal structure of LMWPTPase of microbial origin, the first of its kind from Mycobacterium tuberculosis. The structure was determined to be two crystal forms at 1.9- and 2.5-A resolutions. These structural forms are compared with those of the LMWPTPases of eukaryotes. Though the overall structure resembles that of the eukaryotic LMWPTPases, there are significant changes around the active site and the protein tyrosine phosphatase (PTP) loop. The variable loop forming the wall of the crevice leading to the active site is conformationally unchanged from that of mammalian LMWPTPase; however, differences are observed in the residues involved, suggesting that they have a role in influencing different substrate specificities. The single amino acid substitution (Leu12Thr [underlined below]) in the consensus sequence of the PTP loop, CTGNICRS, has a major role in the stabilization of the PTP loop, unlike what occurs in mammalian LMWPTPases. A chloride ion and a glycerol molecule were modeled in the active site where the chloride ion interacts in a manner similar to that of phosphate with the main chain nitrogens of the PTP loop. This structural study, in addition to identifying specific mycobacterial features, may also form the basis for exploring the mechanism of the substrate specificities of bacterial LMWPTPases.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21530278 K.Chandra, D.Dutta, A.Mitra, A.K.Das, and A.Basak (2011).
Design, synthesis and inhibition activity of a novel cyclic enediyne amino acid conjugates against MPtpA.
  Bioorg Med Chem, 19, 3274-3279.  
19678837 J.Blobel, P.Bernadó, H.Xu, C.Jin, and M.Pons (2009).
Weak oligomerization of low-molecular-weight protein tyrosine phosphatase is conserved from mammals to bacteria.
  FEBS J, 276, 4346-4357.  
19889539 K.A.Rawls, P.T.Lang, J.Takeuchi, S.Imamura, T.D.Baguley, C.Grundner, T.Alber, and J.A.Ellman (2009).
Fragment-based discovery of selective inhibitors of the Mycobacterium tuberculosis protein tyrosine phosphatase PtpA.
  Bioorg Med Chem Lett, 19, 6851-6854.  
17975835 C.Madhurantakam, V.R.Chavali, and A.K.Das (2008).
Analyzing the catalytic mechanism of MPtpA: a low molecular weight protein tyrosine phosphatase from Mycobacterium tuberculosis through site-directed mutagenesis.
  Proteins, 71, 706-714.  
  18474358 H.Bach, K.G.Papavinasasundaram, D.Wong, Z.Hmama, and Y.Av-Gay (2008).
Mycobacterium tuberculosis virulence is mediated by PtpA dephosphorylation of human vacuolar protein sorting 33B.
  Cell Host Microbe, 3, 316-322.  
17372358 M.R.Groves, I.B.Müller, X.Kreplin, and J.Müller-Dieckmann (2007).
A method for the general identification of protein crystals in crystallization experiments using a noncovalent fluorescent dye.
  Acta Crystallogr D Biol Crystallogr, 63, 526-535.
PDB codes: 2ob1 2ob2
17008719 D.Tolkatchev, R.Shaykhutdinov, P.Xu, J.Plamondon, D.C.Watson, N.M.Young, and F.Ni (2006).
Three-dimensional structure and ligand interactions of the low molecular weight protein tyrosine phosphatase from Campylobacter jejuni.
  Protein Sci, 15, 2381-2394.
PDB code: 2gi4
16672613 H.A.Watkins, and E.N.Baker (2006).
Structural and functional analysis of Rv3214 from Mycobacterium tuberculosis, a protein with conflicting functional annotations, leads to its characterization as a phosphatase.
  J Bacteriol, 188, 3589-3599.
PDB code: 2a6p
16452434 H.Xu, B.Xia, and C.Jin (2006).
Solution structure of a low-molecular-weight protein tyrosine phosphatase from Bacillus subtilis.
  J Bacteriol, 188, 1509-1517.
PDB code: 1zgg
16271885 C.Grundner, H.L.Ng, and T.Alber (2005).
Mycobacterium tuberculosis protein tyrosine phosphatase PtpB structure reveals a diverged fold and a buried active site.
  Structure, 13, 1625-1634.
PDB code: 1ywf
16258834 K.Saxena, B.Elshorst, H.Berk, M.Betz, S.Grimme, T.Langer, B.Pescatore, U.Schieborr, M.Vogtherr, and H.Schwalbe (2005).
Backbone NMR assignment of the low-molecular-weight protein tyrosine phosphatase (MPtpA) from Mycobacterium tuberculosis.
  J Biomol NMR, 33, 136.  
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 codes are shown on the right.