1woh
From Proteopedia
(New page: 200px<br /><applet load="1woh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1woh, resolution 1.75Å" /> '''Crystal Structure of...) |
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| - | [[Image:1woh.gif|left|200px]]<br /><applet load="1woh" size=" | + | [[Image:1woh.gif|left|200px]]<br /><applet load="1woh" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1woh, resolution 1.75Å" /> | caption="1woh, resolution 1.75Å" /> | ||
'''Crystal Structure of Agmatinase Reveals Structural Conservation and Inhibition Mechanism of the Ureohydrolase Superfamily'''<br /> | '''Crystal Structure of Agmatinase Reveals Structural Conservation and Inhibition Mechanism of the Ureohydrolase Superfamily'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Agmatine is the product of arginine decarboxylation and can be hydrolyzed | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1WOH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. Active as [http://en.wikipedia.org/wiki/Agmatinase Agmatinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.3.11 3.5.3.11] Full crystallographic information is available from [http:// | + | 1WOH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. Active as [http://en.wikipedia.org/wiki/Agmatinase Agmatinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.3.11 3.5.3.11] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WOH OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Deinococcus radiodurans]] | [[Category: Deinococcus radiodurans]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Ahn, H | + | [[Category: Ahn, H J.]] |
| - | [[Category: Ha, J | + | [[Category: Ha, J Y.]] |
[[Category: Kim, D.]] | [[Category: Kim, D.]] | ||
| - | [[Category: Kim, K | + | [[Category: Kim, K H.]] |
| - | [[Category: Kwon, A | + | [[Category: Kwon, A R.]] |
| - | [[Category: Lee, H | + | [[Category: Lee, H H.]] |
[[Category: Lee, J.]] | [[Category: Lee, J.]] | ||
| - | [[Category: Suh, S | + | [[Category: Suh, S W.]] |
| - | [[Category: Yoon, H | + | [[Category: Yoon, H J.]] |
[[Category: alpha/beta fold]] | [[Category: alpha/beta fold]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:46:32 2008'' |
Revision as of 13:46, 21 February 2008
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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.
About this Structure
1WOH is a Single protein structure of sequence from Deinococcus radiodurans. Active as Agmatinase, with EC number 3.5.3.11 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 Thu Feb 21 15:46:32 2008
Categories: Agmatinase | Deinococcus radiodurans | Single protein | Ahn, H J. | Ha, J Y. | Kim, D. | Kim, K H. | Kwon, A R. | Lee, H H. | Lee, J. | Suh, S W. | Yoon, H J. | Alpha/beta fold
