We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1eud

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1eud.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1eud.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1eud| PDB=1eud | SCENE= }}
{{STRUCTURE_1eud| PDB=1eud | SCENE= }}
-
'''CRYSTAL STRUCTURE OF PHOSPHORYLATED PIG HEART, GTP-SPECIFIC SUCCINYL-COA SYNTHETASE'''
+
===CRYSTAL STRUCTURE OF PHOSPHORYLATED PIG HEART, GTP-SPECIFIC SUCCINYL-COA SYNTHETASE===
-
==Overview==
+
<!--
-
Succinyl-CoA synthetase (SCS) catalyzes the reversible phosphorylation/dephosphorylation reaction: inverted question mark inverted question mark inverted question markrm succinyl inverted question markhbox inverted question mark- inverted question markCoA+NDP+P_i inverted question markleftrightarrow succinate+CoA+NTP inverted question mark inverted question markwhere N denotes adenosine or guanosine. In the course of the reaction, an essential histidine residue is transiently phosphorylated. We have crystallized and solved the structure of the GTP-specific isoform of SCS from pig heart (EC 6.2.1.4) in both the dephosphorylated and phosphorylated forms. The structures were refined to 2.1 A resolution. In the dephosphorylated structure, the enzyme is stabilized via coordination of a phosphate ion by the active-site histidine residue and the two "power" helices, one contributed by each subunit of the alphabeta-dimer. Small changes in the conformations of residues at the amino terminus of the power helix contributed by the alpha-subunit allow the enzyme to accommodate either the covalently bound phosphoryl group or the free phosphate ion. Structural comparisons are made between the active sites in these two forms of the enzyme, both of which can occur along the catalytic path. Comparisons are also made with the structure of Escherichia coli SCS. The domain that has been shown to bind ADP in E. coli SCS is more open in the pig heart, GTP-specific SCS structure.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10873456}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10873456 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10873456}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Ligase]]
[[Category: Ligase]]
[[Category: Phosphonohistidine]]
[[Category: Phosphonohistidine]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:31:35 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 02:00:04 2008''

Revision as of 23:00, 30 June 2008

Image:1eud.png

Template:STRUCTURE 1eud

CRYSTAL STRUCTURE OF PHOSPHORYLATED PIG HEART, GTP-SPECIFIC SUCCINYL-COA SYNTHETASE

Template:ABSTRACT PUBMED 10873456

About this Structure

1EUD is a Protein complex structure of sequences from Sus scrofa. Full crystallographic information is available from OCA.

Reference

Phosphorylated and dephosphorylated structures of pig heart, GTP-specific succinyl-CoA synthetase., Fraser ME, James MN, Bridger WA, Wolodko WT, J Mol Biol. 2000 Jun 23;299(5):1325-39. PMID:10873456

Page seeded by OCA on Tue Jul 1 02:00:04 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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