2NZ2

Crystal structure of human argininosuccinate synthase in complex with aspartate and citrulline

Summary for 2NZ2

• Entry DOI: 10.2210/pdb2nz2/pdb
• Descriptor: Argininosuccinate synthase, SODIUM ION, ASPARTIC ACID, ... (5 entities in total)
• Functional Keywords: amino-acid biosynthesis, synthase, aspartate, citrulline, structural genomics, structural genomics consortium, sgc, ligase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm, cytosol : P00966
• Total number of polymer chains: 1
• Total formula weight: 47011.63

Authors

Karlberg, T.,Uppenberg, J.,Arrowsmith, C.,Berglund, H.,Busam, R.D.,Collins, R.,Edwards, A.,Ericsson, U.B.,Flodin, S.,Flores, A.,Graslund, S.,Hallberg, B.M.,Hammarstrom, M.,Hogbom, M.,Johansson, I.,Kotenyova, T.,Magnusdottir, A.,Moche, M.,Nilsson, M.E.,Nordlund, P.,Nyman, T.,Ogg, D.,Persson, C.,Sagemark, J.,Stenmark, P.,Sundstrom, M.,Thorsell, A.G.,Van Den Berg, S.,Wallden, K.,Weigelt, J.,Holmberg-Schiavone, L.,Structural Genomics Consortium (SGC) (deposition date: 2006-11-22, release date: 2006-12-05, Last modification date: 2023-11-15)

Primary citation

Karlberg, T.,Collins, R.,van den Berg, S.,Flores, A.,Hammarstrom, M.,Hogbom, M.,Holmberg Schiavone, L.,Uppenberg, J.
Structure of human argininosuccinate synthetase.
Acta Crystallogr.,Sect.D, 64:279-286, 2008

PubMed Abstract: Argininosuccinate synthetase catalyzes the transformation of citrulline and aspartate into argininosuccinate and pyrophosphate using the hydrolysis of ATP to AMP and pyrophosphate. This enzymatic process constitutes the rate-limiting step in both the urea and arginine-citrulline cycles. Previous studies have investigated the crystal structures of argininosuccinate synthetase from bacterial species. In this work, the first crystal structure of human argininosuccinate synthetase in complex with the substrates citrulline and aspartate is presented. The human enzyme is compared with structures of argininosuccinate synthetase from bacteria. In addition, the structure also provides new insights into the function of the numerous clinical mutations identified in patients with type I citrullinaemia (also known as classic citrullinaemia).

PubMed: 18323623
DOI: 10.1107/S0907444907067455

Experimental method

X-RAY DIFFRACTION (2.4 Å)