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1w55

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[[Image:1w55.gif|left|200px]]<br /><applet load="1w55" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1w55.gif|left|200px]]
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caption="1w55, resolution 2.303&Aring;" />
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'''STRUCTURE OF THE BIFUNCTIONAL ISPDF FROM CAMPYLOBACTER JEJUNI'''<br />
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{{Structure
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|PDB= 1w55 |SIZE=350|CAPTION= <scene name='initialview01'>1w55</scene>, resolution 2.303&Aring;
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|SITE= <scene name='pdbsite=AC1:Edo+Binding+Site+For+Chain+A'>AC1</scene>
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=C:CYTIDINE-5'-MONOPHOSPHATE'>C</scene>, <scene name='pdbligand=GPP:GERANYL+DIPHOSPHATE'>GPP</scene> and <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''STRUCTURE OF THE BIFUNCTIONAL ISPDF FROM CAMPYLOBACTER JEJUNI'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1W55 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Campylobacter_jejuni Campylobacter jejuni] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=C:'>C</scene>, <scene name='pdbligand=GPP:'>GPP</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Edo+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W55 OCA].
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1W55 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Campylobacter_jejuni Campylobacter jejuni]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W55 OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15466439 15466439]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15466439 15466439]
[[Category: Campylobacter jejuni]]
[[Category: Campylobacter jejuni]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: bifunctional enzyme]]
[[Category: bifunctional enzyme]]
[[Category: biosynthetic pathway]]
[[Category: biosynthetic pathway]]
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[[Category: isoprenoids]]
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[[Category: isoprenoid]]
[[Category: nonmevalonate]]
[[Category: nonmevalonate]]
[[Category: transferase]]
[[Category: transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:40:37 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:52:17 2008''

Revision as of 12:52, 20 March 2008

Image:1w55.gif


PDB ID 1w55

Drag the structure with the mouse to rotate
, resolution 2.303Å
Sites:
Ligands: , , and
Coordinates: save as pdb, mmCIF, xml



STRUCTURE OF THE BIFUNCTIONAL ISPDF FROM CAMPYLOBACTER JEJUNI


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

1W55 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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