1g8h: Difference between revisions

New page: left|200px<br /><applet load="1g8h" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g8h, resolution 2.80Å" /> '''ATP SULFURYLASE FROM...
 
No edit summary
Line 1: Line 1:
[[Image:1g8h.gif|left|200px]]<br /><applet load="1g8h" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1g8h.gif|left|200px]]<br /><applet load="1g8h" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1g8h, resolution 2.80&Aring;" />
caption="1g8h, resolution 2.80&Aring;" />
'''ATP SULFURYLASE FROM S. CEREVISIAE: THE TERNARY PRODUCT COMPLEX WITH APS AND PPI'''<br />
'''ATP SULFURYLASE FROM S. CEREVISIAE: THE TERNARY PRODUCT COMPLEX WITH APS AND PPI'''<br />


==Overview==
==Overview==
ATP sulfurylases (ATPSs) are ubiquitous enzymes that catalyse the primary, step of intracellular sulfate activation: the reaction of inorganic, sulfate with ATP to form adenosine-5'-phosphosulfate (APS) and, pyrophosphate (PPi). With the crystal structure of ATPS from the yeast, Saccharomyces cerevisiae, we have solved the first structure of a member, of the ATP sulfurylase family. We have analysed the crystal structure of, the native enzyme at 1.95 Angstroms resolution using multiple isomorphous, replacement (MIR) and, subsequently, the ternary enzyme product complex, with APS and PPi bound to the active site. The enzyme consists of six, identical subunits arranged in two stacked rings in a D:3 symmetric, assembly. Nucleotide binding causes significant conformational changes, which lead to a rigid body structural displacement of domains III and IV, of the ATPS monomer. Despite having similar folds and active site design, examination of the active site of ATPS and comparison with known, structures of related nucleotidylyl transferases reveal a novel ATP, binding mode that is peculiar to ATP sulfurylases.
ATP sulfurylases (ATPSs) are ubiquitous enzymes that catalyse the primary step of intracellular sulfate activation: the reaction of inorganic sulfate with ATP to form adenosine-5'-phosphosulfate (APS) and pyrophosphate (PPi). With the crystal structure of ATPS from the yeast Saccharomyces cerevisiae, we have solved the first structure of a member of the ATP sulfurylase family. We have analysed the crystal structure of the native enzyme at 1.95 Angstroms resolution using multiple isomorphous replacement (MIR) and, subsequently, the ternary enzyme product complex with APS and PPi bound to the active site. The enzyme consists of six identical subunits arranged in two stacked rings in a D:3 symmetric assembly. Nucleotide binding causes significant conformational changes, which lead to a rigid body structural displacement of domains III and IV of the ATPS monomer. Despite having similar folds and active site design, examination of the active site of ATPS and comparison with known structures of related nucleotidylyl transferases reveal a novel ATP binding mode that is peculiar to ATP sulfurylases.


==About this Structure==
==About this Structure==
1G8H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with CD, CA, NA, MG, ADX, POP and ACY as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Sulfate_adenylyltransferase Sulfate adenylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.4 2.7.7.4] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1G8H OCA].  
1G8H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=CD:'>CD</scene>, <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=NA:'>NA</scene>, <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=ADX:'>ADX</scene>, <scene name='pdbligand=POP:'>POP</scene> and <scene name='pdbligand=ACY:'>ACY</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Sulfate_adenylyltransferase Sulfate adenylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.4 2.7.7.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G8H OCA].  


==Reference==
==Reference==
Line 16: Line 16:
[[Category: Blaesse, M.]]
[[Category: Blaesse, M.]]
[[Category: Huber, R.]]
[[Category: Huber, R.]]
[[Category: Ullrich, T.C.]]
[[Category: Ullrich, T C.]]
[[Category: ACY]]
[[Category: ACY]]
[[Category: ADX]]
[[Category: ADX]]
Line 31: Line 31:
[[Category: rossmann-fold]]
[[Category: rossmann-fold]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:48:53 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:47:15 2008''

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA