1IV4

Structure of 2C-Methyl-D-erythritol-2,4-cyclodiphosphate Synthase (bound form Substrate)

Summary for 1IV4

• Entry DOI: 10.2210/pdb1iv4/pdb
• Related: 1IV1 1IV2 1IV3
• Descriptor: 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase, MAGNESIUM ION, CYTIDINE-5'-MONOPHOSPHATE, ... (4 entities in total)
• Functional Keywords: isoprenoid, non-mevalonate, synthase, riken structural genomics/proteomics initiative, rsgi, structural genomics, lyase
• Biological source: Thermus thermophilus
• Total number of polymer chains: 6
• Total formula weight: 101819.99

Authors

Kishida, H.,Wada, T.,Unzai, S.,Kuzuyama, T.,Terada, T.,Sirouzu, M.,Yokoyama, S.,Tame, J.R.H.,Park, S.-Y.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2002-03-11, release date: 2002-09-11, Last modification date: 2023-12-27)

Primary citation

Kishida, H.,Wada, T.,Unzai, S.,Kuzuyama, T.,Takagi, M.,Terada, T.,Shirouzu, M.,Yokoyama, S.,Tame, J.R.,Park, S.Y.
Structure and catalytic mechanism of 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (MECDP) synthase, an enzyme in the non-mevalonate pathway of isoprenoid synthesis.
Acta Crystallogr.,Sect.D, 59:23-31, 2003

PubMed Abstract: Precursors for isoprenoid synthesis are essential in all organisms. These compounds are synthesized by one of two known routes: the well characterized mevalonate pathway or a recently discovered non-mevalonate route which is used in many bacteria and human pathogens. Since the second pathway is both vital and unlike any found in humans, enzymes catalysing reactions along this synthetic route are possible drug targets. The structure of one such enzyme from the thermophilic bacterium Thermus thermophilus has been solved to high resolution in the presence of substrate and with a substrate analogue. Enzyme co-crystallized with substrate shows only one product, cytosine monophosphate (CMP), in the active site. At the high resolution of the refinement (1.6 A) the positions and coordination of the magnesium ions in the active site are clearly seen.

PubMed: 12499535
DOI: 10.1107/S0907444902017705

Experimental method

X-RAY DIFFRACTION (1.55 Å)