1aos
From Proteopedia
(Difference between revisions)
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<StructureSection load='1aos' size='340' side='right'caption='[[1aos]], [[Resolution|resolution]] 4.20Å' scene=''> | <StructureSection load='1aos' size='340' side='right'caption='[[1aos]], [[Resolution|resolution]] 4.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1aos]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1aos]] 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=1AOS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AOS 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]] 4.2Å</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=1aos FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aos OCA], [https://pdbe.org/1aos PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aos RCSB], [https://www.ebi.ac.uk/pdbsum/1aos PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aos 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=1aos FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aos OCA], [https://pdbe.org/1aos PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aos RCSB], [https://www.ebi.ac.uk/pdbsum/1aos PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aos ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Disease == | == Disease == | ||
| - | + | [https://www.uniprot.org/uniprot/ARLY_HUMAN ARLY_HUMAN] Defects in ASL are the cause of arginosuccinic aciduria (ARGINSA) [MIM:[https://omim.org/entry/207900 207900]. An autosomal recessive disorder of the urea cycle. The disease is characterized by mental and physical retardation, liver enlargement, skin lesions, dry and brittle hair showing trichorrhexis nodosa microscopically and fluorescing red, convulsions, and episodic unconsciousness.<ref>PMID:1705937</ref> <ref>PMID:2263616</ref> <ref>PMID:12408190</ref> <ref>PMID:17326097</ref> | |
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ARLY_HUMAN ARLY_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=1aos 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=1aos ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Intragenic complementation has been observed at the argininosuccinate lyase (ASL) locus. Intragenic complementation is a phenomenon that occurs when a multimeric protein is formed from subunits produced by different mutant alleles of a gene. The resulting hybrid protein exhibits enzymatic activity that is greater than that found in the oligomeric proteins produced by each mutant allele alone. The mutations involved in the most successful complementation event observed in ASL deficiency were found to be an aspartate to glycine mutation at codon 87 of one allele (D87G) coupled with a glutamine to arginine mutation at codon 286 of the other (Q286R). To understand the structural basis of the Q286R:D87G intragenic complementation event at the ASL locus, we have determined the x-ray crystal structure of recombinant human ASL at 4. 0 A resolution. The structure has been refined to an R factor of 18. 8%. Two monomers related by a noncrystallographic 2-fold axis comprise the asymmetric unit, and a crystallographic 2-fold axis of space group P3121 completes the tetramer. Each of the four active sites is composed of residues from three monomers. Structural mapping of the Q286R and D87G mutations indicate that both are near the active site and each is contributed by a different monomer. Thus when mutant monomers combine randomly such that one active site contains both mutations, it is required by molecular symmetry that another active site exists with no mutations. These "native" active sites give rise to the observed partial recovery of enzymatic activity. | ||
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| - | Human argininosuccinate lyase: a structural basis for intragenic complementation.,Turner MA, Simpson A, McInnes RR, Howell PL Proc Natl Acad Sci U S A. 1997 Aug 19;94(17):9063-8. PMID:9256435<ref>PMID:9256435</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1aos" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Homo sapiens]] |
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[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Howell | + | [[Category: Howell PL]] |
| - | [[Category: Mcinnes | + | [[Category: Mcinnes RR]] |
| - | [[Category: Simpson | + | [[Category: Simpson A]] |
| - | [[Category: Turner | + | [[Category: Turner MA]] |
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Current revision
HUMAN ARGININOSUCCINATE LYASE
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