The crystal structure of murine CMP-5-N-acetylneuraminic acid synthetase. 2003

Stephan Krapp, and Anja K Münster-Kühnel, and Jens T Kaiser, and Robert Huber, and Joe Tiralongo, and Rita Gerardy-Schahn, and Uwe Jacob
Max-Planck-Institut für Biochemie, Abteilung für Strukturforschung, Am Klopferspitz 18a, 82152, Martinsried, Germany.

Sialic acids are activated by CMP-5-N-acetylneuraminic acid synthetase prior to their transfer onto oligo- or polysaccharides. Here, we present the crystal structure of the N-terminal catalytically active domain of the murine 5-N-acetylneuraminic acid synthetase in complex with the reaction product. In contrast to the previously solved structure of 5-N-acetylneuraminic acid synthetase from Neisseria meningitidis and the related CMP-KDO-synthetase of Escherichia coli, the murine enzyme is a tetramer, which was observed with the active sites closed. In this conformation a loop is shifted by 6A towards the active site and thus an essential arginine residue can participate in catalysis. Furthermore, a network of intermolecular salt-bridges and hydrogen bonds in the dimer as well as hydrophobic interfaces between two dimers indicate a cooperative behaviour of the enzyme. In addition, a complex regulation of the enzyme activity is proposed that includes phosphorylation and dephosphorylation.

UI MeSH Term Description Entries
D008958 Models, Molecular Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures. Molecular Models,Model, Molecular,Molecular Model
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D011485 Protein Binding The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments. Plasma Protein Binding Capacity,Binding, Protein
D011487 Protein Conformation The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain). Conformation, Protein,Conformations, Protein,Protein Conformations
D003569 Cytidine Monophosphate N-Acetylneuraminic Acid A nucleoside monophosphate sugar which donates N-acetylneuraminic acid to the terminal sugar of a ganglioside or glycoprotein. CMP Acetylneuraminic Acid,CMP-N-Acetylneuraminic Acid,CMP-NANA,D-glycero-beta-D-galacto-2-Nonulopyranosonic acid, 5-(acetylamino)-3,5-dideoxy-, 2-(hydrogen 5'-cytidylate),CMP-Sialic Acid,Cytidine Monophosphate N Acetylneuraminic Acid,Acetylneuraminic Acid, CMP,CMP N Acetylneuraminic Acid,CMP Sialic Acid
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000216 N-Acylneuraminate Cytidylyltransferase An enzyme that forms CMP-acylneuraminic acids, which donate the N-acylneuraminic acid residues to the terminal sugar residue of a ganglioside or glycoprotein. EC 2.7.7.43. Acylneuraminate Cytidylyltransferase,CMP Sialate Pyrophosphorylase,CMP Sialate Synthase,CMP-N-Acetylneuraminic Acid Synthetase,CMP-Sialic Acid Synthetase,Cytidine 5'-Monophosphosialic Acid Synthetase,Cytidine 5-Monophosphosialate Synthase,CMP N Acetylneuraminic Acid Synthetase,CMP Sialic Acid Synthetase,Cytidine 5 Monophosphosialate Synthase,Cytidine 5' Monophosphosialic Acid Synthetase,Cytidylyltransferase, Acylneuraminate,Cytidylyltransferase, N-Acylneuraminate,N Acylneuraminate Cytidylyltransferase,Pyrophosphorylase, CMP Sialate,Sialate Pyrophosphorylase, CMP,Sialate Synthase, CMP,Synthase, CMP Sialate,Synthase, Cytidine 5-Monophosphosialate,Synthetase, CMP-N-Acetylneuraminic Acid,Synthetase, CMP-Sialic Acid
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D001426 Bacterial Proteins Proteins found in any species of bacterium. Bacterial Gene Products,Bacterial Gene Proteins,Gene Products, Bacterial,Bacterial Gene Product,Bacterial Gene Protein,Bacterial Protein,Gene Product, Bacterial,Gene Protein, Bacterial,Gene Proteins, Bacterial,Protein, Bacterial,Proteins, Bacterial

Related Publications

Stephan Krapp, and Anja K Münster-Kühnel, and Jens T Kaiser, and Robert Huber, and Joe Tiralongo, and Rita Gerardy-Schahn, and Uwe Jacob
March 1991, Glycobiology,
Stephan Krapp, and Anja K Münster-Kühnel, and Jens T Kaiser, and Robert Huber, and Joe Tiralongo, and Rita Gerardy-Schahn, and Uwe Jacob
December 1994, Journal of bacteriology,
Stephan Krapp, and Anja K Münster-Kühnel, and Jens T Kaiser, and Robert Huber, and Joe Tiralongo, and Rita Gerardy-Schahn, and Uwe Jacob
May 1999, Glycobiology,
Stephan Krapp, and Anja K Münster-Kühnel, and Jens T Kaiser, and Robert Huber, and Joe Tiralongo, and Rita Gerardy-Schahn, and Uwe Jacob
November 2002, Sheng wu gong cheng xue bao = Chinese journal of biotechnology,
Stephan Krapp, and Anja K Münster-Kühnel, and Jens T Kaiser, and Robert Huber, and Joe Tiralongo, and Rita Gerardy-Schahn, and Uwe Jacob
September 1989, The Journal of biological chemistry,
Stephan Krapp, and Anja K Münster-Kühnel, and Jens T Kaiser, and Robert Huber, and Joe Tiralongo, and Rita Gerardy-Schahn, and Uwe Jacob
August 2016, Molecular medicine reports,
Stephan Krapp, and Anja K Münster-Kühnel, and Jens T Kaiser, and Robert Huber, and Joe Tiralongo, and Rita Gerardy-Schahn, and Uwe Jacob
January 2006, Biochemical and biophysical research communications,
Stephan Krapp, and Anja K Münster-Kühnel, and Jens T Kaiser, and Robert Huber, and Joe Tiralongo, and Rita Gerardy-Schahn, and Uwe Jacob
July 1973, Biochimica et biophysica acta,
Stephan Krapp, and Anja K Münster-Kühnel, and Jens T Kaiser, and Robert Huber, and Joe Tiralongo, and Rita Gerardy-Schahn, and Uwe Jacob
August 1986, The Journal of biological chemistry,
Stephan Krapp, and Anja K Münster-Kühnel, and Jens T Kaiser, and Robert Huber, and Joe Tiralongo, and Rita Gerardy-Schahn, and Uwe Jacob
October 1983, The Biochemical journal,
Copied contents to your clipboard!