PDBsum entry 3ogz

Transferase

PDB id: 3ogz

Contents

Protein chain

578 a.a. *

Ligands

GOL

Waters ×397

* Residue conservation analysis

PDB id:

3ogz

Name:

Transferase

Title:

Protein structure of usp from l. Major in apo-form

Structure:

Udp-sugar pyrophosphorylase. Chain: a. Engineered: yes

Source:

Leishmania major. Organism_taxid: 5664. Strain: 5askh. Gene: usp. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

2.03Å R-factor: 0.186 R-free: 0.220

Authors:

A.Dickmanns,S.Damerow,P.Neumann,E.-C.Schulz,A.Lamerz,F.Routier, R.Ficner

Key ref:

A.Dickmanns et al. (2011). Structural basis for the broad substrate range of the UDP-sugar pyrophosphorylase from Leishmania major. J Mol Biol, 405, 461-478. PubMed id: 21073876

Date:

17-Aug-10 Release date: 17-Nov-10

Protein chain

D3G6S4  (D3G6S4_LEIMA) -  UTP-monosaccharide-1-phosphate uridylyltransferase from Leishmania major

Seq: 630 a.a.

Struc: 578 a.a.

Enzyme reactions

• Enzyme class: E.C.2.7.7.64 - UTP-monosaccharide-1-phosphate uridylyltransferase.
• Reaction: a monosaccharide 1-phosphate + UTP + H⁺ = a UDP-monosaccharide + diphosphate
• Cofactor: Mn(2+) or Mg(2+)

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

Added reference

J Mol Biol 405:461-478 (2011)

PubMed id: 21073876

Structural basis for the broad substrate range of the UDP-sugar pyrophosphorylase from Leishmania major.

A.Dickmanns, S.Damerow, P.Neumann, E.C.Schulz, A.C.Lamerz, F.H.Routier, R.Ficner.

ABSTRACT

Nucleotide sugars and the enzymes that are responsible for their synthesis are indispensable for the production of complex carbohydrates and, thus, for elaboration of a protective cellular coat for many organisms such as the protozoan parasite Leishmania. These activated sugars are synthesized de novo or derived from salvaged monosaccharides. In addition to UDP-glucose (UDP-Glc) pyrophosphorylase, which catalyzes the formation of UDP-Glc from substrates UTP and glucose-1-phosphate, Leishmania major and plants express a UDP-sugar pyrophosphorylase (USP) that exhibits broad substrate specificity in vitro. The enzyme, likely involved in monosaccharide salvage, preferentially generates UDP-Glc and UDP-galactose, but it may also activate other hexose- or pentose-1-phosphates such as galacturonic acid-1-phosphate or arabinose-1-phosphate. In order to gain insight into structural features governing the differences in substrate specificity, we determined the crystal structure of the L. major USP in the APO-, UTP-, and UDP-sugar-bound conformations. The overall tripartite structure of USP exhibits a significant structural homology to other nucleotidyldiphosphate-glucose pyrophosphorylases. The obtained USP structures reveal the structural rearrangements occurring during the stepwise binding process of the substrates. Moreover, the different product complexes explain the broad substrate specificity of USP, which is enabled by structural changes in the sugar binding region of the active site.