1d9e

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|PDB= 1d9e |SIZE=350|CAPTION= <scene name='initialview01'>1d9e</scene>, resolution 2.4&Aring;
|PDB= 1d9e |SIZE=350|CAPTION= <scene name='initialview01'>1d9e</scene>, resolution 2.4&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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|ACTIVITY= [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]
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|ACTIVITY= <span class='plainlinks'>[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] </span>
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1d9e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d9e OCA], [http://www.ebi.ac.uk/pdbsum/1d9e PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1d9e RCSB]</span>
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[[Category: Radaev, S.]]
[[Category: Radaev, S.]]
[[Category: Woodard, R W.]]
[[Category: Woodard, R W.]]
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[[Category: SO4]]
 
[[Category: a5p]]
[[Category: a5p]]
[[Category: dah7p]]
[[Category: dah7p]]
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[[Category: tim barrel]]
[[Category: tim barrel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:34:50 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:37:08 2008''

Revision as of 16:37, 30 March 2008


PDB ID 1d9e

Drag the structure with the mouse to rotate
, resolution 2.4Å
Ligands:
Activity: 3-deoxy-8-phosphooctulonate synthase, with EC number 2.5.1.55
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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. 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

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