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.


1c4t

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1c4t.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1c4t.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1c4t| PDB=1c4t | SCENE= }}
{{STRUCTURE_1c4t| PDB=1c4t | SCENE= }}
-
'''CATALYTIC DOMAIN FROM TRIMERIC DIHYDROLIPOAMIDE SUCCINYLTRANSFERASE'''
+
===CATALYTIC DOMAIN FROM TRIMERIC DIHYDROLIPOAMIDE SUCCINYLTRANSFERASE===
-
==Overview==
+
<!--
-
The dihydrolipoamide succinyltransferase (E2o) component of the alpha-ketoglutarate dehydrogenase complex catalyzes the transfer of a succinyl group from the S-succinyldihydrolipoyl moiety to coenzyme A. E2o is normally a 24-mer, but is found as a trimer when E2o is expressed with a C-terminal [His]6 tag. The crystal structure of the trimeric form of the catalytic domain (CD) of the Escherichia coli E2o has been solved to 3.0 A resolution using the Molecular Replacement method. The refined model contains an intact trimer in the asymmetric unit and has an R-factor of 0.257 (Rfree = 0.286) for 18,699 reflections between 10.0 and 3.0 A resolution. The core of tE2oCD (residues 187-396) superimposes onto that of the cubic E2oCD with an RMS difference of 0.4 A for all main-chain atoms. The C-terminal end of tE2oCD (residues 397-404) rotates by an average of 37 degrees compared to cubic E2oCD, disrupting the normal twofold interface. Despite the alteration of quaternary structure, the active site of tE2oCD shows no significant differences from that of the cubic E2oCD, although several side chains in the active site are more ordered in the trimeric form of E2oCD. Analysis of the available sequence data suggests that the majority of E2 components have active sites that resemble that of E. coli E2oCD. The remaining E2 components can be divided into three groups based on active-site sequence similarity. Analysis of the surface properties of both crystal forms of E. coli E2oCD suggests key residues that may be involved in the protein-protein contacts that occur between the catalytic and lipoyl domains of E2o.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10739245}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10739245 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10739245}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Ketoglutarate dehydrogenase multienzyme complex]]
[[Category: Ketoglutarate dehydrogenase multienzyme complex]]
[[Category: Transferase]]
[[Category: Transferase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:19:42 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:12:27 2008''

Revision as of 17:12, 30 June 2008

Image:1c4t.png

Template:STRUCTURE 1c4t

CATALYTIC DOMAIN FROM TRIMERIC DIHYDROLIPOAMIDE SUCCINYLTRANSFERASE

Template:ABSTRACT PUBMED 10739245

About this Structure

1C4T is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Expression, purification, and structural analysis of the trimeric form of the catalytic domain of the Escherichia coli dihydrolipoamide succinyltransferase., Knapp JE, Carroll D, Lawson JE, Ernst SR, Reed LJ, Hackert ML, Protein Sci. 2000 Jan;9(1):37-48. PMID:10739245

Page seeded by OCA on Mon Jun 30 20:12:27 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1c4t"
Personal tools