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<StructureSection load='2pha' size='340' side='right'caption='[[2pha]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='2pha' size='340' side='right'caption='[[2pha]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2pha]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2pha]] 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=2PHA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PHA FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> | ||
<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> | |||
<tr id=' | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2pha FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pha OCA], [https://pdbe.org/2pha PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pha RCSB], [https://www.ebi.ac.uk/pdbsum/2pha PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pha ProSAT]</span></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=2pha FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pha OCA], [https://pdbe.org/2pha PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pha RCSB], [https://www.ebi.ac.uk/pdbsum/2pha PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pha ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Disease == | == 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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=2pha ConSurf]. | </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=2pha ConSurf]. | ||
<div style="clear:both"></div> | <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. | |||
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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2pha" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Christianson | [[Category: Christianson DW]] | ||
[[Category: Costanzo | [[Category: Di Costanzo L]] | ||
[[Category: Pique | [[Category: Pique ME]] | ||
Latest revision as of 14:01, 30 August 2023
Crystal structure of native, unliganded human arginase at 1.90 resolutionCrystal structure of native, unliganded human arginase at 1.90 resolution
Structural highlights
DiseaseARGI1_HUMAN Defects in ARG1 are the cause of argininemia (ARGIN) [MIM: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.[1] [2] FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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