This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1j70

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1j70.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1j70.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1j70| PDB=1j70 | SCENE= }}
{{STRUCTURE_1j70| PDB=1j70 | SCENE= }}
-
'''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.
 +
-->
 +
{{ABSTRACT_PUBMED_14983089}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Tang, H.]]
[[Category: Tang, H.]]
[[Category: Nucleotide binding fold and kinase fold]]
[[Category: Nucleotide binding fold and kinase fold]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:51:37 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 14:34:03 2008''

Revision as of 11:34, 1 July 2008

Image:1j70.png

Template:STRUCTURE 1j70

CRYSTAL STRUCTURE OF YEAST ATP SULFURYLASE

Template:ABSTRACT PUBMED 14983089

About this Structure

1J70 is a Single protein structure of sequence from Saccharomyces cerevisiae. 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 Tue Jul 1 14:34:03 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1j70"
Personal tools