PDBsum entry 2htb

Isomerase

PDB id: 2htb

Contents

Protein chains

296 a.a. *

Waters ×322

* Residue conservation analysis

PDB id:

2htb

Name:

Isomerase

Title:

Crystal structure of a putative mutarotase (yead) from salmonella typhimurium in monoclinic form

Structure:

Putative enzyme related to aldose 1-epimerase. Chain: a, b, c, d. Engineered: yes

Source:

Salmonella typhimurium. Organism_taxid: 602. Strain: ifo12529. Gene: yead. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.50Å R-factor: 0.191 R-free: 0.240

Authors:

S.Chittori,D.K.Simanshu,H.S.Savithri,M.R.N.Murthy

Key ref:

S.Chittori et al. (2007). Structure of the putative mutarotase YeaD from Salmonella typhimurium: structural comparison with galactose mutarotases. Acta Crystallogr D Biol Crystallogr, 63, 197-205. PubMed id: 17242513 DOI: 10.1107/S090744490604618X

Date:

25-Jul-06 Release date: 23-Jan-07

Protein chains

Q8ZPV9  (YEAD_SALTY) -  Putative glucose-6-phosphate 1-epimerase from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)

Seq: 294 a.a.

Struc: 296 a.a.

Enzyme reactions

• Enzyme class: E.C.5.1.3.15 - glucose-6-phosphate 1-epimerase.
• Reaction: alpha-D-glucose 6-phosphate = beta-D-glucose 6-phosphate

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

Added reference

DOI no: 10.1107/S090744490604618X

Acta Crystallogr D Biol Crystallogr 63:197-205 (2007)

PubMed id: 17242513

Structure of the putative mutarotase YeaD from Salmonella typhimurium: structural comparison with galactose mutarotases.

S.Chittori, D.K.Simanshu, H.S.Savithri, M.R.Murthy.

ABSTRACT

Salmonella typhimurium YeaD (stYeaD), annotated as a putative aldose 1-epimerase, has a very low sequence identity to other well characterized mutarotases. Sequence analysis suggested that the catalytic residues and a few of the substrate-binding residues of galactose mutarotases (GalMs) are conserved in stYeaD. Determination of the crystal structure of stYeaD in an orthorhombic form at 1.9 A resolution and in a monoclinic form at 2.5 A resolution revealed this protein to adopt the beta-sandwich fold similar to GalMs. Structural comparison of stYeaD with GalMs has permitted the identification of residues involved in catalysis and substrate binding. In spite of the similar fold and conservation of catalytic residues, minor but significant differences were observed in the substrate-binding pocket. These analyses pointed out the possible role of Arg74 and Arg99, found only in YeaD-like proteins, in ligand anchoring and suggested that the specificity of stYeaD may be distinct from those of GalMs.

Selected figure(s)

Figure 3.
Figure 3 Superposition of the active-site residues of (a) stYeaD and lacGalM and (b) stYeaD and YMR099cp. Colour code: green, lacGalM; wheat, stYeaD; pink; YMR099cp.

The above figure is reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2007, 63, 197-205) copyright 2007.

Figure was selected by an automated process.