1jcx

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[[Image:1jcx.gif|left|200px]]<br /><applet load="1jcx" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1jcx.gif|left|200px]]
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caption="1jcx, resolution 1.80&Aring;" />
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'''Aquifex aeolicus KDO8P synthase in complex with API and Cadmium'''<br />
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{{Structure
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|PDB= 1jcx |SIZE=350|CAPTION= <scene name='initialview01'>1jcx</scene>, resolution 1.80&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene> and <scene name='pdbligand=PAI:{[(2,2-DIHYDROXY-ETHYL)-(2,3,4,5-TETRAHYDROXY-6-PHOSPHONOOXY-HEXYL)-AMINO]-METHYL}-PHOSPHONIC ACID'>PAI</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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|GENE=
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}}
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'''Aquifex aeolicus KDO8P synthase in complex with API and Cadmium'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1JCX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus] with <scene name='pdbligand=CD:'>CD</scene> and <scene name='pdbligand=PAI:'>PAI</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1JCX OCA].
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1JCX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JCX OCA].
==Reference==
==Reference==
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Structures of Aquifex aeolicus KDO8P synthase in complex with R5P and PEP, and with a bisubstrate inhibitor: role of active site water in catalysis., Wang J, Duewel HS, Woodard RW, Gatti DL, Biochemistry. 2001 Dec 25;40(51):15676-83. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11747443 11747443]
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Structures of Aquifex aeolicus KDO8P synthase in complex with R5P and PEP, and with a bisubstrate inhibitor: role of active site water in catalysis., Wang J, Duewel HS, Woodard RW, Gatti DL, Biochemistry. 2001 Dec 25;40(51):15676-83. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11747443 11747443]
[[Category: 3-deoxy-8-phosphooctulonate synthase]]
[[Category: 3-deoxy-8-phosphooctulonate synthase]]
[[Category: Aquifex aeolicus]]
[[Category: Aquifex aeolicus]]
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[[Category: kdo]]
[[Category: kdo]]
[[Category: kdo8p]]
[[Category: kdo8p]]
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[[Category: kdo8ps]]
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[[Category: kdo8p]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:21:14 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:01:42 2008''

Revision as of 10:01, 20 March 2008


PDB ID 1jcx

Drag the structure with the mouse to rotate
, resolution 1.80Å
Ligands: and
Activity: 3-deoxy-8-phosphooctulonate synthase, with EC number 2.5.1.55
Coordinates: save as pdb, mmCIF, xml



Aquifex aeolicus KDO8P synthase in complex with API and Cadmium


Overview

We have determined the crystal structures of the metalloenzyme 3-deoxy-D-manno-octulosonate 8-phosphate (KDO8P) synthase from Aquifex aeolicus in complex with phosphoenolpyruvate (PEP) and ribose 5-phosphate (R5P), and with a bisubstrate inhibitor that mimics the postulated linear reaction intermediate. R5P, which is not a substrate for KDO8P synthase, binds in a manner similar to that of arabinose 5-phosphate (A5P), which is the natural substrate. The lack of reactivity of R5P appears to be primarily a consequence of the loss of a water molecule coordinated to Cd(2+) and located on the si side of PEP. This water molecule is no longer present because it cannot form a hydrogen bond with C2-OH(R5P), which is oriented in a different direction from C2-OH(A5P). The bisubstrate inhibitor binds with its phosphate and phosphonate moieties occupying the positions of the phosphate groups of A5P and PEP, respectively. One of the inhibitor hydroxyls replaces water as a ligand of Cd(2+). The current work supports a mechanism for the synthesis of KDO8P, in which a hydroxide ion on the si side of PEP attacks C2(PEP), forming a tetrahedral-like intermediate with a buildup of negative charge at C3(PEP). The ensuing condensation of C3(PEP) with C1(A5P) would be favored by a proton transfer from the phosphate moiety of PEP to the aldehyde carbonyl of A5P to generate the hydroxyl. Overall, the process can be described as a syn addition of water and A5P to the si side of PEP.

About this Structure

1JCX is a Single protein structure of sequence from Aquifex aeolicus. Full crystallographic information is available from OCA.

Reference

Structures of Aquifex aeolicus KDO8P synthase in complex with R5P and PEP, and with a bisubstrate inhibitor: role of active site water in catalysis., Wang J, Duewel HS, Woodard RW, Gatti DL, Biochemistry. 2001 Dec 25;40(51):15676-83. PMID:11747443

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