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.


1tmi

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1tmi.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1tmi.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1tmi| PDB=1tmi | SCENE= }}
{{STRUCTURE_1tmi| PDB=1tmi | SCENE= }}
-
'''Structure of Thermotoga maritima S63A non-processing mutant S-adenosylmethionine decarboxylase'''
+
===Structure of Thermotoga maritima S63A non-processing mutant S-adenosylmethionine decarboxylase===
-
==Overview==
+
<!--
-
S-adenosylmethionine decarboxylase (AdoMetDC) is a critical regulatory enzyme of the polyamine biosynthetic pathway and belongs to a small class of pyruvoyl-dependent amino acid decarboxylases. Structural elucidation of the prokaryotic AdoMetDC is of substantial interest in order to determine the relationship between the eukaryotic and prokaryotic forms of the enzyme. Although both forms utilize pyruvoyl groups, there is no detectable sequence similarity except at the site of pyruvoyl group formation. The x-ray structure of the Thermatoga maritima AdoMetDC proenzyme reveals a dimeric protein fold that is remarkably similar to the eukaryotic AdoMetDC protomer, suggesting an evolutionary link between the two forms of the enzyme. Three key active site residues (Ser55, His68, and Cys83) involved in substrate binding, catalysis or proenzyme processing that were identified in the human and potato AdoMet-DCs are structurally conserved in the T. maritima AdoMetDC despite very limited primary sequence identity. The role of Ser55, His68, and Cys83 in the self-processing reaction was investigated through site-directed mutagenesis. A homology model for the Escherichia coli AdoMetDC was generated based on the structures of the T. maritima and human AdoMetDCs.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15150268}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15150268 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15150268}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Toms, A V.]]
[[Category: Toms, A V.]]
[[Category: Two-layer alpha beta-sandwich]]
[[Category: Two-layer alpha beta-sandwich]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:07:46 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:41:54 2008''

Revision as of 14:41, 27 July 2008

Image:1tmi.png

Template:STRUCTURE 1tmi

Structure of Thermotoga maritima S63A non-processing mutant S-adenosylmethionine decarboxylase

Template:ABSTRACT PUBMED 15150268

About this Structure

1TMI is a Single protein structure of sequence from Thermotoga maritima. Full crystallographic information is available from OCA.

Reference

Evolutionary links as revealed by the structure of Thermotoga maritima S-adenosylmethionine decarboxylase., Toms AV, Kinsland C, McCloskey DE, Pegg AE, Ealick SE, J Biol Chem. 2004 Aug 6;279(32):33837-46. Epub 2004 May 18. PMID:15150268

Page seeded by OCA on Sun Jul 27 17:41:54 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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