1j70: Difference between revisions

Revision as of 14:34, 1 July 2008

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File:1j70.png

Template:STRUCTURE 1j70

CRYSTAL STRUCTURE OF YEAST ATP SULFURYLASECRYSTAL STRUCTURE OF YEAST ATP SULFURYLASE

Template:ABSTRACT PUBMED 14983089

About this StructureAbout this Structure

1J70 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

ReferenceReference

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

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-'''CRYSTAL STRUCTURE OF YEAST ATP SULFURYLASE'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_14983089}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 14983089 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_14983089}}
 ==About this Structure==
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 [[Category: Tang, H.]]
 [[Category: Nucleotide binding fold and kinase fold]]
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