1gqc

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{{STRUCTURE_1gqc| PDB=1gqc | SCENE= }}
{{STRUCTURE_1gqc| PDB=1gqc | SCENE= }}
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'''THE STRUCTURE OF CMP:2-KETO-3-DEOXY-MANNO-OCTONIC ACID SYNTHETASE COMPLEXED WITH CMP-KDO AT 100K'''
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===THE STRUCTURE OF CMP:2-KETO-3-DEOXY-MANNO-OCTONIC ACID SYNTHETASE COMPLEXED WITH CMP-KDO AT 100K===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 11802716 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11802716}}
==About this Structure==
==About this Structure==
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[[Category: Nucleotidyltransferase]]
[[Category: Nucleotidyltransferase]]
[[Category: Sugar-activating enzyme]]
[[Category: Sugar-activating enzyme]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 05:53:28 2008''

Revision as of 02:53, 1 July 2008

Image:1gqc.png

Template:STRUCTURE 1gqc

THE STRUCTURE OF CMP:2-KETO-3-DEOXY-MANNO-OCTONIC ACID SYNTHETASE COMPLEXED WITH CMP-KDO AT 100K

Template:ABSTRACT PUBMED 11802716

About this Structure

1GQC 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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