5hdm: Difference between revisions
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==Crystal structure of Arabidopsis thaliana glutamate-1-semialdehyde-2,1-aminomutase== | |||
<StructureSection load='5hdm' size='340' side='right'caption='[[5hdm]], [[Resolution|resolution]] 1.25Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5hdm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HDM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HDM FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.25Å</td></tr> | |||
<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>, <scene name='pdbligand=PMP:4-DEOXY-4-AMINOPYRIDOXAL-5-PHOSPHATE'>PMP</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=5hdm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hdm OCA], [https://pdbe.org/5hdm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hdm RCSB], [https://www.ebi.ac.uk/pdbsum/5hdm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hdm ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/GSA1_ARATH GSA1_ARATH] Transaminase converting glutamate 1-semialdehyde (GSA) to 5-aminolevulinate (ALA). Involved in the biosynthesis of tetrapyrroles.<ref>PMID:7908550</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Glutamate-1-semialdehyde-2,1-aminomutase (GSAM) catalyzes the isomerization of glutamate-1-semialdehyde (GSA) to 5-aminolevulinate (ALA) and is distributed in archaea, most bacteria and plants. Although structures of GSAM from archaea and bacteria have been resolved, a GSAM structure from a higher plant is not available, preventing further structure-function analysis. Here, the structure of GSAM from Arabidopsis thaliana (AtGSA1) obtained by X-ray crystallography is reported at 1.25 A resolution. AtGSA1 forms an asymmetric dimer and displays asymmetry in cofactor binding as well as in the gating-loop orientation, which is consistent with previously reported Synechococcus GSAM structures. While one monomer binds PMP with the gating loop fixed in the open state, the other monomer binds either PMP or PLP and the gating loop is ready to close. The data also reveal the mobility of residues Gly163, Ser164 and Gly165, which are important for reorientation of the gating loop. Furthermore, the asymmetry of the AtGSA1 structure supports the previously proposed negative cooperativity between monomers of GSAM. | |||
Crystal structure of glutamate-1-semialdehyde-2,1-aminomutase from Arabidopsis thaliana.,Song Y, Pu H, Jiang T, Zhang L, Ouyang M Acta Crystallogr F Struct Biol Commun. 2016 Jun;72(Pt 6):448-56. doi:, 10.1107/S2053230X16007263. Epub 2016 May 23. PMID:27303897<ref>PMID:27303897</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5hdm" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Aminomutase 3D structures|Aminomutase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Arabidopsis thaliana]] | |||
[[Category: Large Structures]] | |||
[[Category: Liu L]] | |||
[[Category: Pu H]] | |||
[[Category: Song Y]] | |||
Latest revision as of 10:32, 9 August 2023
Crystal structure of Arabidopsis thaliana glutamate-1-semialdehyde-2,1-aminomutaseCrystal structure of Arabidopsis thaliana glutamate-1-semialdehyde-2,1-aminomutase
Structural highlights
FunctionGSA1_ARATH Transaminase converting glutamate 1-semialdehyde (GSA) to 5-aminolevulinate (ALA). Involved in the biosynthesis of tetrapyrroles.[1] Publication Abstract from PubMedGlutamate-1-semialdehyde-2,1-aminomutase (GSAM) catalyzes the isomerization of glutamate-1-semialdehyde (GSA) to 5-aminolevulinate (ALA) and is distributed in archaea, most bacteria and plants. Although structures of GSAM from archaea and bacteria have been resolved, a GSAM structure from a higher plant is not available, preventing further structure-function analysis. Here, the structure of GSAM from Arabidopsis thaliana (AtGSA1) obtained by X-ray crystallography is reported at 1.25 A resolution. AtGSA1 forms an asymmetric dimer and displays asymmetry in cofactor binding as well as in the gating-loop orientation, which is consistent with previously reported Synechococcus GSAM structures. While one monomer binds PMP with the gating loop fixed in the open state, the other monomer binds either PMP or PLP and the gating loop is ready to close. The data also reveal the mobility of residues Gly163, Ser164 and Gly165, which are important for reorientation of the gating loop. Furthermore, the asymmetry of the AtGSA1 structure supports the previously proposed negative cooperativity between monomers of GSAM. Crystal structure of glutamate-1-semialdehyde-2,1-aminomutase from Arabidopsis thaliana.,Song Y, Pu H, Jiang T, Zhang L, Ouyang M Acta Crystallogr F Struct Biol Commun. 2016 Jun;72(Pt 6):448-56. doi:, 10.1107/S2053230X16007263. Epub 2016 May 23. PMID:27303897[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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