1gq9
From Proteopedia
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|PDB= 1gq9 |SIZE=350|CAPTION= <scene name='initialview01'>1gq9</scene>, resolution 2.6Å | |PDB= 1gq9 |SIZE=350|CAPTION= <scene name='initialview01'>1gq9</scene>, resolution 2.6Å | ||
|SITE= <scene name='pdbsite=CTA:Ctp+Binding+Site+For+Chain+B'>CTA</scene> | |SITE= <scene name='pdbsite=CTA:Ctp+Binding+Site+For+Chain+B'>CTA</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CTP:CYTIDINE-5'-TRIPHOSPHATE'>CTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/3-deoxy-manno-octulosonate_cytidylyltransferase 3-deoxy-manno-octulosonate cytidylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.38 2.7.7.38] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/3-deoxy-manno-octulosonate_cytidylyltransferase 3-deoxy-manno-octulosonate cytidylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.38 2.7.7.38] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gq9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gq9 OCA], [http://www.ebi.ac.uk/pdbsum/1gq9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gq9 RCSB]</span> | ||
}} | }} | ||
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[[Category: Jelakovic, S.]] | [[Category: Jelakovic, S.]] | ||
[[Category: Schulz, G E.]] | [[Category: Schulz, G E.]] | ||
| - | [[Category: CTP]] | ||
| - | [[Category: MG]] | ||
[[Category: cmp-kdo synthetase]] | [[Category: cmp-kdo synthetase]] | ||
[[Category: lipopolysaccharide biosynthesis]] | [[Category: lipopolysaccharide biosynthesis]] | ||
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[[Category: sugar-activating enzyme]] | [[Category: sugar-activating enzyme]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:49:14 2008'' |
Revision as of 17:49, 30 March 2008
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| , resolution 2.6Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , | ||||||
| Activity: | 3-deoxy-manno-octulosonate cytidylyltransferase, with EC number 2.7.7.38 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE STRUCTURE OF CMP:2-KETO-3-DEOXY-MANNO-OCTONIC ACID SYNTHETASE COMPLEXED WITH CTP AT 100K
Overview
The activation of the sugar 2-keto-3-deoxy-manno-octonic acid (Kdo) is catalyzed by CMP-Kdo synthetase (EC 2.7.7.38) and results in a monophosphate diester with CMP. The enzyme is a pharmaceutical target because CMP-Kdo is required for the biosynthesis of lipopolysaccharides that are vital for Gram-negative bacteria. We have established the structures of an enzyme complex with the educt CTP and of a complex with the product CMP-Kdo by X-ray diffraction analyses at 100 K, both at 2.6 A resolution. The N-terminal domains of the dimeric enzyme bind CTP in a peculiar nucleotide-binding fold with the beta- and gamma-phosphates located at the so-called "PP-loop", whereas the C-terminal domains participate in Kdo binding and in the dimer interface. The unstable nucleotide-sugar CMP-Kdo was produced in a crystal and stabilized by freezing to 100 K. Its formation is accompanied by an induced fit involving mainchain displacements in the 2 A range. The observed binding conformations together with the amino acid conservation pattern during evolution and the putative location of the required Mg(2+) ion suggest a reaction pathway. The enzyme is structurally homologous to the CMP-N-acetylneuraminic acid synthetases in all parts except for the dimer interface. Moreover, the chainfold and the substrate-binding positions resemble those of other enzymes processing nucleotide sugars.
About this Structure
1GQ9 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Catalytic mechanism of CMP:2-keto-3-deoxy-manno-octonic acid synthetase as derived from complexes with reaction educt and product., Jelakovic S, Schulz GE, Biochemistry. 2002 Jan 29;41(4):1174-81. PMID:11802716
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