PDBsum entry: 1h3m

Transferase

PDB id: 1h3m

Contents

Protein chains

215 a.a. *

Ligands

N2P

Metals

_CL ×5

Waters ×86

* Residue conservation analysis

PDB id:

1h3m

Name:

Transferase

Title:

Structure of 4-diphosphocytidyl-2c-methyl-d-erythritol synthetase

Structure:

2-c-methyl-d-erythritol 4-phosphate cytidylyltransferase. Chain: a, b. Engineered: yes. Mutation: yes

Source:

Escherichia coli. Organism_taxid: 469008. Strain: bl21(de3). Expressed in: escherichia coli. Expression_system_taxid: 469008.

Biol. unit:

Dimer (from PDB file)

Resolution:

2.4Å R-factor: 0.241 R-free: 0.333

Authors:

L.E.Kemp,C.S.Bond,W.N.Hunter

Key ref:

L.E.Kemp et al. (2003). Structure of a tetragonal crystal form of Escherichia coli 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase. Acta Crystallogr D Biol Crystallogr, 59, 607-610. PubMed id: 12595740 DOI: 10.1107/S090744490202365X

Date:

10-Sep-02 Release date: 01-Aug-03

Protein chains

Q46893  (ISPD_ECOLI) -  2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase

Seq: 236 a.a.

Struc: 215 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.2.7.7.60 - 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase.
• Reaction: CTP + 2-C-methyl-D-erythritol 4-phosphate = diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
• Cofactor: Manganese or magnesium

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

 Gene Ontology (GO) functional annotation 

• Biological process: isoprenoid biosynthetic process (2 terms)
• Biochemical function: catalytic activity (4 terms)

reference

DOI no: 10.1107/S090744490202365X

Acta Crystallogr D Biol Crystallogr 59:607-610 (2003)

PubMed id: 12595740

Structure of a tetragonal crystal form of Escherichia coli 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase.

L.E.Kemp, C.S.Bond, W.N.Hunter.

ABSTRACT

2-C-Methyl-D-erythritol 4-phosphate cytidylyltransferase is an essential enzyme in the mevalonate-independent pathway of isoprenoid biosynthesis. The structure of a tetragonal crystal form has been solved by molecular replacement and refined to 2.4 A resolution. Structure and sequence comparisons suggest that the enzyme is a suitable target for a structure-based approach to the development of novel broad-spectrum antibiotics. However, the absence of ligands in the enzyme active site together with the moderate resolution of the structure indicates that this tetragonal crystal form is inferior to that of a previously reported highly ordered monoclinic form [Richard et al. (2001), Nature Struct. Biol. 8, 641-647].

Selected figure(s)

Figure 1.
Figure 1 Stereoview C^ trace of the MEPC dimer (subunit A, cyan; subunit B, black). One active site (subunit B) is labelled and the C^ positions of strictly conserved residues around this active site are depicted as red spheres. Every 20th C^ position starting from residue 10, with the exception of residue 190B, is depicted as a black sphere and numbered in black for subunit A and in blue for subunit B. Residue Asp190B is strictly conserved in MEPC and is depicted with a red sphere at the active site.

The above figure is reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2003, 59, 607-610) copyright 2003.

Figure was selected by the author.