4cbs

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'''Unreleased structure'''
 
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The entry 4cbs is ON HOLD until Paper Publication
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==X-ray structure of quintuple mutant of human alanine glyoxylate aminotransferase, AGXT_RHEAM==
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<StructureSection load='4cbs' size='340' side='right'caption='[[4cbs]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4cbs]] is a 1 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=4CBS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CBS FirstGlance]. <br>
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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]] 2.3&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
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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=4cbs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cbs OCA], [https://pdbe.org/4cbs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cbs RCSB], [https://www.ebi.ac.uk/pdbsum/4cbs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cbs ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/AGT1_HUMAN AGT1_HUMAN] Primary hyperoxaluria type 1. The disease is caused by variants affecting the gene represented in this entry.
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== Function ==
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[https://www.uniprot.org/uniprot/AGT1_HUMAN AGT1_HUMAN] Peroxisomal aminotransferase that catalyzes the transamination of glyoxylate to glycine and contributes to the glyoxylate detoxification (PubMed:10960483, PubMed:12777626, PubMed:24055001, PubMed:23229545, PubMed:26149463). Also catalyzes the transamination between L-serine and pyruvate and contributes to gluconeogenesis from the L-serine metabolism (PubMed:10347152).<ref>PMID:10347152</ref> <ref>PMID:10960483</ref> <ref>PMID:12777626</ref> <ref>PMID:23229545</ref> <ref>PMID:24055001</ref> <ref>PMID:26149463</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Protein stability is a fundamental issue in biomedical and biotechnological applications of proteins. Among them, gene- and enzyme-replacement strategies are promising approaches to treat inherited diseases that may benefit from protein engineering techniques, even though these beneficial effects have been largely unexplored. We apply here a sequence-alignment statistics procedure (consensus-based approach) to improve the activity and stability of the human alanine:glyoxylate aminotransferase (AGT) protein, an enzyme which causes primary hyperoxaluria type I (PH1) upon mutation. By combining only five consensus mutations, we obtain a variant (AGT-RHEAM) with largely enhanced in vitro thermal and kinetic stability, increased activity and no side effects on foldability and peroxisomal targeting in mammalian cells. The structure of AGT-RHEAM reveals changes at the dimer interface and improved electrostatic interactions responsible for increased kinetic stability. Consensus-based variants maintain the overall protein fold, crystallized more easily and improve the expression as soluble proteins in two different systems (AGT and CIPK24/SOS2). Thus, the consensus-based approach also emerges as a simple and generic strategy to increase the crystallization success for hard-to-get protein targets as well as to enhance protein stability and function for biomedical applications.
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Authors: Yunta, C., Albert, A.
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The consensus-based approach for gene/enzyme replacement therapies and crystallization strategies: the case of human alanine:glyoxylate aminotransferase.,Mesa-Torres N, Yunta C, Fabelo-Rosa I, Gonzalez-Rubio JM, Sanchez-Ruiz JM, Salido E, Albert A, Pey AL Biochem J. 2014 Jun 24. PMID:24957194<ref>PMID:24957194</ref>
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Description: X-ray structure of quintuple mutant of human alanine glyoxylate aminotransferase, AGXT_RHEAM
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4cbs" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Aminotransferase 3D structures|Aminotransferase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Albert A]]
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[[Category: Yunta C]]

Current revision

X-ray structure of quintuple mutant of human alanine glyoxylate aminotransferase, AGXT_RHEAM

PDB ID 4cbs

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