1H3M

Structure of 4-diphosphocytidyl-2C-methyl-D-erythritol synthetase

Summary for 1H3M

• Entry DOI: 10.2210/pdb1h3m/pdb
• Related: 1I52 1INI 1INJ
• Descriptor: 2-C-METHYL-D-ERYTHRITOL 4-PHOSPHATE CYTIDYLYLTRANSFERASE, CHLORIDE ION, PENTANE-1,5-DIAMINE, ... (4 entities in total)
• Functional Keywords: transferase, isoprenoid, synthetase
• Biological source: ESCHERICHIA COLI
• Total number of polymer chains: 2
• Total formula weight: 51621.64

Authors

Kemp, L.E.,Bond, C.S.,Hunter, W.N. (deposition date: 2002-09-10, release date: 2003-08-01, Last modification date: 2023-12-13)

Primary citation

Kemp, L.E.,Bond, C.S.,Hunter, W.N.
Structure of a Tetragonal Crystal Form of Escherichia Coli 2-C-Methyl-D-Erythritol 4-Phosphate Cytidylyltransferase
Acta Crystallogr.,Sect.D, 59:607-, 2003

PubMed 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].

PubMed: 12595740
DOI: 10.1107/S090744490202365X

Experimental method

X-RAY DIFFRACTION (2.4 Å)