1d9e
From Proteopedia
(New page: 200px<br /><applet load="1d9e" size="450" color="white" frame="true" align="right" spinBox="true" caption="1d9e, resolution 2.4Å" /> '''STRUCTURE OF E. COLI ...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1d9e.jpg|left|200px]]<br /><applet load="1d9e" size=" | + | [[Image:1d9e.jpg|left|200px]]<br /><applet load="1d9e" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1d9e, resolution 2.4Å" /> | caption="1d9e, resolution 2.4Å" /> | ||
'''STRUCTURE OF E. COLI KDO8P SYNTHASE'''<br /> | '''STRUCTURE OF E. COLI KDO8P SYNTHASE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | 3-deoxy-D-manno-octulosonate 8-phosphate (KDO8P) synthase catalyzes the | + | 3-deoxy-D-manno-octulosonate 8-phosphate (KDO8P) synthase catalyzes the condensation of phosphoenolpyruvate (PEP) with arabinose 5-phosphate (A5P) to form KDO8P and inorganic phosphate. KDO8P is the phosphorylated precursor of 3-deoxy-D-manno-octulosonate, an essential sugar of the lipopolysaccharide of Gram-negative bacteria. The crystal structure of the Escherichia coli KDO8P synthase has been determined by multiple wavelength anomalous diffraction and the model has been refined to 2.4 A (R-factor, 19.9%; R-free, 23.9%). KDO8P synthase is a homotetramer in which each monomer has the fold of a (beta/alpha)(8) barrel. On the basis of the features of the active site, PEP and A5P are predicted to bind with their phosphate moieties 13 A apart such that KDO8P synthesis would proceed via a linear intermediate. A reaction similar to KDO8P synthesis, the condensation of phosphoenolpyruvate, and erythrose 4-phosphate to form 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAH7P), is catalyzed by DAH7P synthase. In the active site of DAH7P synthase the two substrates PEP and erythrose 4-phosphate appear to bind in a configuration similar to that proposed for PEP and A5P in the active site of KDO8P synthase. This observation suggests that KDO8P synthase and DAH7P synthase evolved from a common ancestor and that they adopt the same catalytic strategy. |
==About this Structure== | ==About this Structure== | ||
| - | 1D9E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/3-deoxy-8-phosphooctulonate_synthase 3-deoxy-8-phosphooctulonate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.55 2.5.1.55] Full crystallographic information is available from [http:// | + | 1D9E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/3-deoxy-8-phosphooctulonate_synthase 3-deoxy-8-phosphooctulonate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.55 2.5.1.55] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D9E OCA]. |
==Reference== | ==Reference== | ||
| Line 15: | Line 15: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Dastidar, P.]] | [[Category: Dastidar, P.]] | ||
| - | [[Category: Gatti, D | + | [[Category: Gatti, D L.]] |
[[Category: Patel, M.]] | [[Category: Patel, M.]] | ||
[[Category: Radaev, S.]] | [[Category: Radaev, S.]] | ||
| - | [[Category: Woodard, R | + | [[Category: Woodard, R W.]] |
[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: a5p]] | [[Category: a5p]] | ||
| Line 27: | Line 27: | ||
[[Category: tim barrel]] | [[Category: tim barrel]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:14:23 2008'' |
Revision as of 10:14, 21 February 2008
|
STRUCTURE OF E. COLI KDO8P SYNTHASE
Overview
3-deoxy-D-manno-octulosonate 8-phosphate (KDO8P) synthase catalyzes the condensation of phosphoenolpyruvate (PEP) with arabinose 5-phosphate (A5P) to form KDO8P and inorganic phosphate. KDO8P is the phosphorylated precursor of 3-deoxy-D-manno-octulosonate, an essential sugar of the lipopolysaccharide of Gram-negative bacteria. The crystal structure of the Escherichia coli KDO8P synthase has been determined by multiple wavelength anomalous diffraction and the model has been refined to 2.4 A (R-factor, 19.9%; R-free, 23.9%). KDO8P synthase is a homotetramer in which each monomer has the fold of a (beta/alpha)(8) barrel. On the basis of the features of the active site, PEP and A5P are predicted to bind with their phosphate moieties 13 A apart such that KDO8P synthesis would proceed via a linear intermediate. A reaction similar to KDO8P synthesis, the condensation of phosphoenolpyruvate, and erythrose 4-phosphate to form 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAH7P), is catalyzed by DAH7P synthase. In the active site of DAH7P synthase the two substrates PEP and erythrose 4-phosphate appear to bind in a configuration similar to that proposed for PEP and A5P in the active site of KDO8P synthase. This observation suggests that KDO8P synthase and DAH7P synthase evolved from a common ancestor and that they adopt the same catalytic strategy.
About this Structure
1D9E is a Single protein structure of sequence from Escherichia coli with as ligand. Active as 3-deoxy-8-phosphooctulonate synthase, with EC number 2.5.1.55 Full crystallographic information is available from OCA.
Reference
Structure and mechanism of 3-deoxy-D-manno-octulosonate 8-phosphate synthase., Radaev S, Dastidar P, Patel M, Woodard RW, Gatti DL, J Biol Chem. 2000 Mar 31;275(13):9476-84. PMID:10734095
Page seeded by OCA on Thu Feb 21 12:14:23 2008
Categories: 3-deoxy-8-phosphooctulonate synthase | Escherichia coli | Single protein | Dastidar, P. | Gatti, D L. | Patel, M. | Radaev, S. | Woodard, R W. | SO4 | A5p | Dah7p | Kdo | Kdo8p | Pep | Tim barrel
