2zav: Difference between revisions

No edit summary
No edit summary
 
(11 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:2zav.gif|left|200px]]


{{Structure
==Arginase I (homo sapiens): native and unliganded structure at 1.70 A resolution==
|PDB= 2zav |SIZE=350|CAPTION= <scene name='initialview01'>2zav</scene>, resolution 1.70&Aring;
<StructureSection load='2zav' size='340' side='right'caption='[[2zav]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>
<table><tr><td colspan='2'>[[2zav]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZAV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZAV FirstGlance]. <br>
|ACTIVITY= <span class='plainlinks'>[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] </span>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
|GENE=
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2zav FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zav OCA], [https://pdbe.org/2zav PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zav RCSB], [https://www.ebi.ac.uk/pdbsum/2zav PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zav ProSAT]</span></td></tr>
|RELATEDENTRY=[[2pha|2PHA]]
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2zav FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zav OCA], [http://www.ebi.ac.uk/pdbsum/2zav PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2zav RCSB]</span>
== Disease ==
}}
[https://www.uniprot.org/uniprot/ARGI1_HUMAN ARGI1_HUMAN] Defects in ARG1 are the cause of argininemia (ARGIN) [MIM:[https://omim.org/entry/207800 207800]; also known as hyperargininemia. Argininemia is a rare autosomal recessive disorder of the urea cycle. Arginine is elevated in the blood and cerebrospinal fluid, and periodic hyperammonemia occurs. Clinical manifestations include developmental delay, seizures, mental retardation, hypotonia, ataxia, progressive spastic quadriplegia.<ref>PMID:1463019</ref> <ref>PMID:7649538</ref>
== Function ==
[https://www.uniprot.org/uniprot/ARGI1_HUMAN ARGI1_HUMAN]
== 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/za/2zav_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=2zav ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structure of the human arginase I-thiosemicarbazide complex reveals an unusual thiocarbonyl mu-sulfide ligand in the binuclear manganese cluster. The C=S moiety of thiosemicarbazide bridges Mn(2+)A and Mn(2+)B with coordination distances of 2.6 A and 2.4 A, respectively. Otherwise, the binding of thiosemicarbazide to human arginase I does not cause any significant structural changes in the active site. The crystal structure of the unliganded enzyme reveals a hydrogen bonded water molecule that could support proton transfer between a mu-water molecule and H141 to regenerate the nucleophilic mu-hydroxide ion in the final step of catalysis.


'''Arginase I (homo sapiens): native and unliganded structure at 1.70 A resolution'''
Crystal structure of human arginase I complexed with thiosemicarbazide reveals an unusual thiocarbonyl mu-sulfide ligand in the binuclear manganese cluster.,Di Costanzo L, Pique ME, Christianson DW J Am Chem Soc. 2007 May 23;129(20):6388-9. doi: 10.1021/ja071567j. Epub 2007 May , 1. PMID:17469833<ref>PMID:17469833</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2zav" style="background-color:#fffaf0;"></div>


==About this Structure==
==See Also==
2ZAV is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZAV OCA].
*[[Arginase 3D structures|Arginase 3D structures]]
 
== References ==
==Reference==
<references/>
Crystal structure of human arginase I complexed with thiosemicarbazide reveals an unusual thiocarbonyl mu-sulfide ligand in the binuclear manganese cluster., Di Costanzo L, Pique ME, Christianson DW, J Am Chem Soc. 2007 May 23;129(20):6388-9. Epub 2007 May 1. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17469833 17469833]
__TOC__
[[Category: Arginase]]
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Christianson, D W.]]
[[Category: Christianson DW]]
[[Category: Costanzo, L Di.]]
[[Category: Di Costanzo L]]
[[Category: alternative splicing]]
[[Category: apical water]]
[[Category: arginine metabolism]]
[[Category: cytoplasm]]
[[Category: disease mutation]]
[[Category: hydrolase]]
[[Category: manganese cluster coordination]]
[[Category: metal-binding]]
[[Category: phosphorylation]]
[[Category: polymorphism]]
[[Category: proton wire]]
[[Category: urea cycle]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:19:58 2008''

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA