1woi

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1woi.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1woi.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1woi| PDB=1woi | SCENE= }}
{{STRUCTURE_1woi| PDB=1woi | SCENE= }}
-
'''Crystal Structure of Agmatinase Reveals Structural Conservation and Inhibition Mechanism of the Ureohydrolase Superfamily'''
+
===Crystal Structure of Agmatinase Reveals Structural Conservation and Inhibition Mechanism of the Ureohydrolase Superfamily===
-
==Overview==
+
<!--
-
Agmatine is the product of arginine decarboxylation and can be hydrolyzed by agmatinase to putrescine, the precursor for biosynthesis of higher polyamines, spermidine, and spermine. Besides being an intermediate in polyamine metabolism, recent findings indicate that agmatine may play important regulatory roles in mammals. Agmatinase is a binuclear manganese metalloenzyme and belongs to the ureohydrolase superfamily that includes arginase, formiminoglutamase, and proclavaminate amidinohydrolase. Compared with a wealth of structural information available for arginases, no three-dimensional structure of agmatinase has been reported. Agmatinase from Deinococcus radiodurans, a 304-residue protein, shows approximately 33% of sequence identity to human mitochondrial agmatinase. Here we report the crystal structure of D. radiodurans agmatinase in Mn(2+)-free, Mn(2+)-bound, and Mn(2+)-inhibitor-bound forms, representing the first structure of agmatinase. It reveals the conservation as well as variation in folding, oligomerization, and the active site of the ureohydrolase superfamily. D. radiodurans agmatinase exists as a compact homohexamer of 32 symmetry. Its binuclear manganese cluster is highly similar but not identical to the clusters of arginase and proclavaminate amidinohydrolase. The structure of the inhibited complex reveals that inhibition by 1,6-diaminohexane arises from the displacement of the metal-bridging water.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15355972}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15355972 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15355972}}
==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Yoon, H J.]]
[[Category: Yoon, H J.]]
[[Category: Alpha/beta fold]]
[[Category: Alpha/beta fold]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:56:54 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:54:08 2008''

Revision as of 04:54, 29 July 2008

Image:1woi.png

Template:STRUCTURE 1woi

Crystal Structure of Agmatinase Reveals Structural Conservation and Inhibition Mechanism of the Ureohydrolase Superfamily

Template:ABSTRACT PUBMED 15355972

About this Structure

1WOI is a Single protein structure of sequence from Deinococcus radiodurans. Full crystallographic information is available from OCA.

Reference

Crystal structure of agmatinase reveals structural conservation and inhibition mechanism of the ureohydrolase superfamily., Ahn HJ, Kim KH, Lee J, Ha JY, Lee HH, Kim D, Yoon HJ, Kwon AR, Suh SW, J Biol Chem. 2004 Nov 26;279(48):50505-13. Epub 2004 Sep 7. PMID:15355972

Page seeded by OCA on Tue Jul 29 07:54:08 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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