1g8h

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|PDB= 1g8h |SIZE=350|CAPTION= <scene name='initialview01'>1g8h</scene>, resolution 2.80&Aring;
|PDB= 1g8h |SIZE=350|CAPTION= <scene name='initialview01'>1g8h</scene>, resolution 2.80&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ADX:ADENOSINE-5&#39;-PHOSPHOSULFATE'>ADX</scene>, <scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</scene> and <scene name='pdbligand=ACY:ACETIC ACID'>ACY</scene>
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|LIGAND= <scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=ADX:ADENOSINE-5&#39;-PHOSPHOSULFATE'>ADX</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</scene>
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|ACTIVITY= [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]
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|ACTIVITY= <span class='plainlinks'>[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] </span>
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=[[1g8f|1G8F]], [[1g8g|1G8G]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g8h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g8h OCA], [http://www.ebi.ac.uk/pdbsum/1g8h PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1g8h RCSB]</span>
}}
}}
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[[Category: Huber, R.]]
[[Category: Huber, R.]]
[[Category: Ullrich, T C.]]
[[Category: Ullrich, T C.]]
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[[Category: ACY]]
 
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[[Category: ADX]]
 
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[[Category: CA]]
 
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[[Category: CD]]
 
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[[Category: MG]]
 
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[[Category: NA]]
 
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[[Category: POP]]
 
[[Category: alpha-beta protein]]
[[Category: alpha-beta protein]]
[[Category: beta-barrel]]
[[Category: beta-barrel]]
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[[Category: rossmann-fold]]
[[Category: rossmann-fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 11:53:55 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:38:48 2008''

Revision as of 17:38, 30 March 2008


PDB ID 1g8h

Drag the structure with the mouse to rotate
, resolution 2.80Å
Ligands: , , , , , ,
Activity: Sulfate adenylyltransferase, with EC number 2.7.7.4
Related: 1G8F, 1G8G


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



ATP SULFURYLASE FROM S. CEREVISIAE: THE TERNARY PRODUCT COMPLEX WITH APS AND PPI


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.

About this Structure

1G8H is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Crystal structure of ATP sulfurylase from Saccharomyces cerevisiae, a key enzyme in sulfate activation., Ullrich TC, Blaesse M, Huber R, EMBO J. 2001 Feb 1;20(3):316-29. PMID:11157739

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