1w57
From Proteopedia
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|PDB= 1w57 |SIZE=350|CAPTION= <scene name='initialview01'>1w57</scene>, resolution 3.091Å | |PDB= 1w57 |SIZE=350|CAPTION= <scene name='initialview01'>1w57</scene>, resolution 3.091Å | ||
|SITE= <scene name='pdbsite=AC1:Gpp+Binding+Site+For+Chain+A'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Gpp+Binding+Site+For+Chain+A'>AC1</scene> | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=C5P:CYTIDINE-5'-MONOPHOSPHATE'>C5P</scene>, <scene name='pdbligand=GPP:GERANYL+DIPHOSPHATE'>GPP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1w57 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w57 OCA], [http://www.ebi.ac.uk/pdbsum/1w57 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1w57 RCSB]</span> | ||
}} | }} | ||
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[[Category: Gabrielsen, M.]] | [[Category: Gabrielsen, M.]] | ||
[[Category: Hunter, W N.]] | [[Category: Hunter, W N.]] | ||
| - | [[Category: C5P]] | ||
| - | [[Category: GPP]] | ||
| - | [[Category: ZN]] | ||
[[Category: bifunctional]] | [[Category: bifunctional]] | ||
[[Category: bifunctional enzyme]] | [[Category: bifunctional enzyme]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:31:24 2008'' |
Revision as of 21:31, 30 March 2008
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| , resolution 3.091Å | |||||||
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| Sites: | |||||||
| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF THE BIFUNCTIONAL ISPDF FROM CAMPYLOBACTER JEJUNI CONTAINING ZN
Overview
The bifunctional methylerythritol 4-phosphate cytidylyltransferase methylerythritol 2,4-cyclodiphosphate synthase (IspDF) is unusual in that it catalyzes nonconsecutive reactions in the 1-deoxy-D-xylulose 5-phosphate (DOXP) pathway of isoprenoid precursor biosynthesis. The crystal structure of IspDF from the bacterial pathogen Campylobacter jejuni reveals an elongated hexamer with D3 symmetry compatible with the dimeric 2C-methyl-D-erythritol-4-phosphate cytidylyltransferase and trimeric 2C-methyl-D-erythritol-2,4-cyclodiphosphate synthase monofunctional enzymes. Complex formation of IspDF with 4-diphosphocytidyl-2C-methyl-D-erythritol kinase (IspE), the intervening enzyme activity in the pathway, has been observed in solution for the enzymes from C. jejuni and Agrobacterium tumefaciens. The monofunctional enzymes (2C-methyl-D-erythritol-4-phosphate cytidylyltransferase, IspE, and 2C-methyl-D-erythritol-2,4-cyclodiphosphate synthase) involved in the DOXP biosynthetic pathway of Escherichia coli also show physical associations. We propose that complex formation of the three enzymes at the core of the DOXP pathway can produce an assembly localizing 18 catalytic centers for the early stages of isoprenoid biosynthesis.
About this Structure
1W57 is a Single protein structure of sequence from Campylobacter jejuni. Full crystallographic information is available from OCA.
Reference
Hexameric assembly of the bifunctional methylerythritol 2,4-cyclodiphosphate synthase and protein-protein associations in the deoxy-xylulose-dependent pathway of isoprenoid precursor biosynthesis., Gabrielsen M, Bond CS, Hallyburton I, Hecht S, Bacher A, Eisenreich W, Rohdich F, Hunter WN, J Biol Chem. 2004 Dec 10;279(50):52753-61. Epub 2004 Oct 2. PMID:15466439
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