1woh

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[[Image:1woh.gif|left|200px]]
 
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{{Structure
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==Crystal Structure of Agmatinase Reveals Structural Conservation and Inhibition Mechanism of the Ureohydrolase Superfamily==
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|PDB= 1woh |SIZE=350|CAPTION= <scene name='initialview01'>1woh</scene>, resolution 1.75&Aring;
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<StructureSection load='1woh' size='340' side='right'caption='[[1woh]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1woh]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WOH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WOH FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</td></tr>
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|GENE=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1woh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1woh OCA], [https://pdbe.org/1woh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1woh RCSB], [https://www.ebi.ac.uk/pdbsum/1woh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1woh ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=[[1wog|1WOG]], [[1woi|1WOI]]
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1woh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1woh OCA], [http://www.ebi.ac.uk/pdbsum/1woh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1woh RCSB]</span>
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[https://www.uniprot.org/uniprot/Q9RZ04_DEIRA Q9RZ04_DEIRA]
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}}
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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'''Crystal Structure of Agmatinase Reveals Structural Conservation and Inhibition Mechanism of the Ureohydrolase Superfamily'''
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wo/1woh_consurf.spt"</scriptWhenChecked>
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==Overview==
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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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.
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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==About this Structure==
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1woh ConSurf].
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1WOH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WOH OCA].
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<div style="clear:both"></div>
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__TOC__
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==Reference==
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</StructureSection>
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15355972 15355972]
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[[Category: Agmatinase]]
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[[Category: Deinococcus radiodurans]]
[[Category: Deinococcus radiodurans]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Ahn, H J.]]
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[[Category: Ahn HJ]]
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[[Category: Ha, J Y.]]
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[[Category: Ha J-Y]]
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[[Category: Kim, D.]]
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[[Category: Kim D]]
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[[Category: Kim, K H.]]
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[[Category: Kim KH]]
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[[Category: Kwon, A R.]]
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[[Category: Kwon A-R]]
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[[Category: Lee, H H.]]
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[[Category: Lee HH]]
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[[Category: Lee, J.]]
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[[Category: Lee J]]
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[[Category: Suh, S W.]]
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[[Category: Suh SW]]
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[[Category: Yoon, H J.]]
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[[Category: Yoon H-J]]
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[[Category: alpha/beta fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:39:01 2008''
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Current revision

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

PDB ID 1woh

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