PDBsum entry: 2a6p

Structural genomics, unknown function

PDB id: 2a6p

Contents

Protein chains

193 a.a. *

Ligands

SO4 ×2

GOL ×2

Waters ×106

* Residue conservation analysis

PDB id:

2a6p

Name:

Structural genomics, unknown function

Title:

Structure solution to 2.2 angstrom and functional characteri the open reading frame rv3214 from mycobacterium tuberculos

Structure:

Possible phosphoglycerate mutase gpm2. Chain: a, b. Synonym: phosphoglyceromutase, pgam, bpg-dependent pgam. Engineered: yes

Source:

Mycobacterium tuberculosis. Organism_taxid: 83332. Strain: h37rv. Gene: rv3214 (entd). Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Biol. unit:

Dimer (from PQS)

Resolution:

2.20Å R-factor: 0.209 R-free: 0.226

Authors:

H.A.Watkins,M.Yu,E.N.Baker,Tb Structural Genomics Consortium

Key ref:

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. PubMed id: 16672613 DOI: 10.1128/JB.188.10.3589-3599.2006

Date:

03-Jul-05 Release date: 16-May-06

Protein chains

Q6MWZ7  (Q6MWZ7_MYCTU) -  POSSIBLE PHOSPHOGLYCERATE MUTASE GPM2 (PHOSPHOGLYCEROMUTASE) (PGAM) (BPG-DEPENDENT PGAM)

Seq: 203 a.a.

Struc: 193 a.a.

Enzyme reactions

• Enzyme class: E.C.5.4.2.1 - Phosphoglycerate mutase.
• Reaction: 2-phospho-D-glycerate = 3-phospho-D-glycerate

2-phospho-D-glycerate (Bound ligand (Het Group name = GOL) matches with 54.55% similarity) = 3-phospho-D-glycerate

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

 Gene Ontology (GO) functional annotation 

• Biochemical function: isomerase activity (4 terms)

Added reference

DOI no: 10.1128/JB.188.10.3589-3599.2006

J Bacteriol 188:3589-3599 (2006)

PubMed id: 16672613

Structural and functional analysis of Rv3214 from Mycobacterium tuberculosis, a protein with conflicting functional annotations, leads to its characterization as a phosphatase.

H.A.Watkins, E.N.Baker.

ABSTRACT

The availability of complete genome sequences has highlighted the problems of functional annotation of the many gene products that have only limited sequence similarity with proteins of known function. The predicted protein encoded by open reading frame Rv3214 from the Mycobacterium tuberculosis H37Rv genome was originally annotated as EntD through sequence similarity with the Escherichia coli EntD, a 4'-phosphopantetheinyl transferase implicated in siderophore biosynthesis. An alternative annotation, based on slightly higher sequence identity, grouped Rv3214 with proteins of the cofactor-dependent phosphoglycerate mutase (dPGM) family. The crystal structure of this protein has been solved by single-wavelength anomalous dispersion methods and refined at 2.07-Angstroms resolution (R = 0.229; R(free) = 0.245). The protein is dimeric, with a monomer fold corresponding to the classical dPGM alpha/beta structure, albeit with some variations. Closer comparisons of structure and sequence indicate that it most closely corresponds with a broad-spectrum phosphatase subfamily within the dPGM superfamily. This functional annotation has been confirmed by biochemical assays which show negligible mutase activity but acid phosphatase activity with a pH optimum of 5.4 and suggests that Rv3214 may be important for mycobacterial phosphate metabolism in vivo. Despite its weak sequence similarity with the 4'-phosphopantetheinyl transferases (EntD homologues), there is little evidence to support this function.