1j70
From Proteopedia
(New page: 200px<br /><applet load="1j70" size="450" color="white" frame="true" align="right" spinBox="true" caption="1j70, resolution 2.30Å" /> '''CRYSTAL STRUCTURE OF...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1j70.jpg|left|200px]]<br /><applet load="1j70" size=" | + | [[Image:1j70.jpg|left|200px]]<br /><applet load="1j70" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1j70, resolution 2.30Å" /> | caption="1j70, resolution 2.30Å" /> | ||
'''CRYSTAL STRUCTURE OF YEAST ATP SULFURYLASE'''<br /> | '''CRYSTAL STRUCTURE OF YEAST ATP SULFURYLASE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | ATP sulfurylase catalyzes the first step in the activation of sulfate by | + | ATP sulfurylase catalyzes the first step in the activation of sulfate by transferring the adenylyl-moiety (AMP approximately ) of ATP to sulfate to form adenosine 5'-phosphosulfate (APS) and pyrophosphate (PP(i)). Subsequently, APS kinase mediates transfer of the gamma-phosphoryl group of ATP to APS to form 3'-phosphoadenosine 5'-phosphosulfate (PAPS) and ADP. The recently determined crystal structure of yeast ATP sulfurylase suggests that its C-terminal domain is structurally quite independent from the other domains, and not essential for catalytic activity. It seems, however, to dictate the oligomerization state of the protein. Here we show that truncation of this domain results in a monomeric enzyme with slightly enhanced catalytic efficiency. Structural alignment of the C-terminal domain indicated that it is extremely similar in its fold to APS kinase although not catalytically competent. While carrying out these structural and functional studies a surface groove was noted. Careful inspection and modeling revealed that the groove is sufficiently deep and wide, as well as properly positioned, to act as a substrate channel between the ATP sulfurylase and APS kinase-like domains of the enzyme. |
==About this Structure== | ==About this Structure== | ||
| - | 1J70 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 PO4 and NA 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:// | + | 1J70 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=PO4:'>PO4</scene> and <scene name='pdbligand=NA:'>NA</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=1J70 OCA]. |
==Reference== | ==Reference== | ||
| Line 15: | Line 15: | ||
[[Category: Sulfate adenylyltransferase]] | [[Category: Sulfate adenylyltransferase]] | ||
[[Category: Dong, A.]] | [[Category: Dong, A.]] | ||
| - | [[Category: Lalor, D | + | [[Category: Lalor, D J.]] |
| - | [[Category: Leyh, T | + | [[Category: Leyh, T S.]] |
| - | [[Category: Pai, E | + | [[Category: Pai, E F.]] |
| - | [[Category: Pilloff, D | + | [[Category: Pilloff, D E.]] |
[[Category: Saridakis, V.]] | [[Category: Saridakis, V.]] | ||
[[Category: Schnyder, T.]] | [[Category: Schnyder, T.]] | ||
| Line 26: | Line 26: | ||
[[Category: nucleotide binding fold and kinase fold]] | [[Category: nucleotide binding fold and kinase fold]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:19:25 2008'' |
Revision as of 11:19, 21 February 2008
|
CRYSTAL STRUCTURE OF YEAST ATP SULFURYLASE
Overview
ATP sulfurylase catalyzes the first step in the activation of sulfate by transferring the adenylyl-moiety (AMP approximately ) of ATP to sulfate to form adenosine 5'-phosphosulfate (APS) and pyrophosphate (PP(i)). Subsequently, APS kinase mediates transfer of the gamma-phosphoryl group of ATP to APS to form 3'-phosphoadenosine 5'-phosphosulfate (PAPS) and ADP. The recently determined crystal structure of yeast ATP sulfurylase suggests that its C-terminal domain is structurally quite independent from the other domains, and not essential for catalytic activity. It seems, however, to dictate the oligomerization state of the protein. Here we show that truncation of this domain results in a monomeric enzyme with slightly enhanced catalytic efficiency. Structural alignment of the C-terminal domain indicated that it is extremely similar in its fold to APS kinase although not catalytically competent. While carrying out these structural and functional studies a surface groove was noted. Careful inspection and modeling revealed that the groove is sufficiently deep and wide, as well as properly positioned, to act as a substrate channel between the ATP sulfurylase and APS kinase-like domains of the enzyme.
About this Structure
1J70 is a Single protein structure of sequence from Saccharomyces cerevisiae with and as ligands. Active as Sulfate adenylyltransferase, with EC number 2.7.7.4 Full crystallographic information is available from OCA.
Reference
Structural and functional analysis of a truncated form of Saccharomyces cerevisiae ATP sulfurylase: C-terminal domain essential for oligomer formation but not for activity., Lalor DJ, Schnyder T, Saridakis V, Pilloff DE, Dong A, Tang H, Leyh TS, Pai EF, Protein Eng. 2003 Dec;16(12):1071-9. PMID:14983089
Page seeded by OCA on Thu Feb 21 13:19:25 2008
