1t4p: Difference between revisions

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[[Image:1t4p.gif|left|200px]]


{{Structure
==Arginase-dehydro-ABH complex==
|PDB= 1t4p |SIZE=350|CAPTION= <scene name='initialview01'>1t4p</scene>, resolution 2.60&Aring;
<StructureSection load='1t4p' size='340' side='right'caption='[[1t4p]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
|SITE=
== Structural highlights ==
|LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> and <scene name='pdbligand=2BH:[(1E,5S)-5-AMINO-5-CARBOXYPENT-1-ENYL](TRIHYDROXY)BORATE(1-)'>2BH</scene>
<table><tr><td colspan='2'>[[1t4p]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T4P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1T4P FirstGlance]. <br>
|ACTIVITY= [http://en.wikipedia.org/wiki/Arginase Arginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.3.1 3.5.3.1]  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
|GENE= ARG1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2BH:[(1E,5S)-5-AMINO-5-CARBOXYPENT-1-ENYL](TRIHYDROXY)BORATE(1-)'>2BH</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
}}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1t4p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t4p OCA], [https://pdbe.org/1t4p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t4p RCSB], [https://www.ebi.ac.uk/pdbsum/1t4p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t4p ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ARGI1_RAT ARGI1_RAT]  
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/t4/1t4p_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1t4p ConSurf].
<div style="clear:both"></div>


'''Arginase-dehydro-ABH complex'''
==See Also==
 
*[[Arginase 3D structures|Arginase 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
Arginase is a manganese metalloenzyme that catalyzes the hydrolysis of L-arginine to form L-ornithine and urea. The structure and stability of the binuclear manganese cluster are critical for catalytic activity as it activates the catalytic nucleophile, metal-bridging hydroxide ion, and stabilizes the tetrahedral intermediate and its flanking states. Here, we report X-ray structures of a series of inhibitors bound to the active site of arginase, and each inhibitor exploits a different mode of coordination with the Mn(2+)(2) cluster. Specifically, we have studied the binding of fluoride ion (F(-); an uncompetitive inhibitor) and L-arginine, L-valine, dinor-N(omega)-hydroxy-L-arginine, descarboxy-nor-N(omega)-hydroxy-L-arginine, and dehydro-2(S)-amino-6-boronohexanoic acid. Some inhibitors, such as fluoride ion, dinor-N(omega)-hydroxy-L-arginine, and dehydro-2(S)-amino-6-boronohexanoic acid, cause the net addition of one ligand to the Mn(2+)(2) cluster. Other inhibitors, such as descarboxy-nor-N(omega)-hydroxy-L-arginine, simply displace the metal-bridging hydroxide ion of the native enzyme and do not cause any net change in the metal coordination polyhedra. The highest affinity inhibitors displace the metal-bridging hydroxide ion (and sometimes occupy a Mn(2+)(A) site found vacant in the native enzyme) and maintain a conserved array of hydrogen bonds with their alpha-amino and -carboxylate groups.
[[Category: Large Structures]]
 
==About this Structure==
1T4P is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T4P OCA].
 
==Reference==
Inhibitor coordination interactions in the binuclear manganese cluster of arginase., Cama E, Pethe S, Boucher JL, Han S, Emig FA, Ash DE, Viola RE, Mansuy D, Christianson DW, Biochemistry. 2004 Jul 20;43(28):8987-99. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15248756 15248756]
[[Category: Arginase]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Ash DE]]
[[Category: Ash, D E.]]
[[Category: Boucher J-L]]
[[Category: Boucher, J L.]]
[[Category: Cama E]]
[[Category: Cama, E.]]
[[Category: Christianson DW]]
[[Category: Christianson, D W.]]
[[Category: Emig FA]]
[[Category: Emig, F A.]]
[[Category: Han S]]
[[Category: Han, S.]]
[[Category: Mansuy D]]
[[Category: Mansuy, D.]]
[[Category: Pethe S]]
[[Category: Pethe, S.]]
[[Category: Viola RE]]
[[Category: Viola, R E.]]
[[Category: 2BH]]
[[Category: MN]]
[[Category: arginase]]
[[Category: dehydro-abh]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:13:46 2008''
Retrieved from "https://proteopedia.org/1t4p"