1xnj
From Proteopedia
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[[Image:1xnj.gif|left|200px]] | [[Image:1xnj.gif|left|200px]] | ||
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'''APS complex of human PAPS synthetase 1''' | '''APS complex of human PAPS synthetase 1''' | ||
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[[Category: Harjes, S.]] | [[Category: Harjes, S.]] | ||
[[Category: Scheidig, A J.]] | [[Category: Scheidig, A J.]] | ||
| - | [[Category: | + | [[Category: Aps kinase]] |
| - | [[Category: | + | [[Category: Atp sulfurylase]] |
| - | [[Category: | + | [[Category: Pap]] |
| - | [[Category: | + | [[Category: Phosphoadenosine phosphosulfate]] |
| - | [[Category: | + | [[Category: Transferase]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:16:03 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 12:16, 3 May 2008
APS complex of human PAPS synthetase 1
Overview
The high energy sulfate donor 3'-phosphoadenosine-5-phosphosulfate (PAPS) is used for sulfate conjugation of extracellular matrix, hormones and drugs. Human PAPS synthetase 1 catalyzes two subsequent reactions starting from ATP and sulfate. First the ATP sulfurylase domain forms APS, then the APS kinase domain phosphorylates the APS intermediate to PAPS. Up to now the interaction between the two enzymatic activities remained elusive, mainly because of missing structural information. Here we present the crystal structure of human PAPSS1 at 1.8 angstroms resolution. The structure reveals a homodimeric, asymmetric complex with the shape of a chair. The two kinase domains adopt different conformational states, with only one being able to bind its two substrates. The asymmetric binding of ADP to the APS kinase is not only observed in the crystal structure, but can also be detected in solution, using an enzymatic assay. These observations strongly indicate structural changes during the reaction cycle. Furthermore crystals soaked with ADP and APS could be prepared and the corresponding structures could be solved.
About this Structure
1XNJ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The crystal structure of human PAPS synthetase 1 reveals asymmetry in substrate binding., Harjes S, Bayer P, Scheidig AJ, J Mol Biol. 2005 Apr 1;347(3):623-35. Epub 2005 Jan 26. PMID:15755455 Page seeded by OCA on Sat May 3 15:16:03 2008
