5dx5: Difference between revisions
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<StructureSection load='5dx5' size='340' side='right'caption='[[5dx5]], [[Resolution|resolution]] 2.37Å' scene=''> | <StructureSection load='5dx5' size='340' side='right'caption='[[5dx5]], [[Resolution|resolution]] 2.37Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5dx5]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5dx5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_sporogenes Clostridium sporogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DX5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DX5 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]] 2.37Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</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=5dx5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dx5 OCA], [https://pdbe.org/5dx5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dx5 RCSB], [https://www.ebi.ac.uk/pdbsum/5dx5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dx5 ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/J7TA22_CLOS1 J7TA22_CLOS1] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
*[[Methionine | *[[Methionine gamma-lyase 3D structures|Methionine gamma-lyase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Clostridium sporogenes]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Anufrieva NV]] | |||
[[Category: Anufrieva | [[Category: Demidkina TV]] | ||
[[Category: Demidkina | [[Category: Morozova EA]] | ||
[[Category: Morozova | [[Category: Nikulin AD]] | ||
[[Category: Nikulin | [[Category: Revtovich SV]] | ||
[[Category: Revtovich | |||
Latest revision as of 01:04, 29 June 2023
Crystal structure of methionine gamma-lyase from Clostridium sporogenesCrystal structure of methionine gamma-lyase from Clostridium sporogenes
Structural highlights
FunctionPublication Abstract from PubMedMethionine gamma-lyase (MGL) is a pyridoxal 5'-phosphate-dependent enzyme that catalyzes the gamma-elimination reaction of L-methionine. The enzyme is a promising target for therapeutic intervention in some anaerobic pathogens and has attracted interest as a potential cancer treatment. The crystal structure of MGL from Clostridium sporogenes has been determined at 2.37 A resolution. The fold of the protein is similar to those of homologous enzymes from Citrobacter freundii, Entamoeba histolytica, Pseudomonas putida and Trichomonas vaginalis. A comparison of these structures revealed differences in the conformation of two flexible regions of the N- and C-terminal domains involved in the active-site architecture. Structure of methionine gamma-lyase from Clostridium sporogenes.,Revtovich S, Anufrieva N, Morozova E, Kulikova V, Nikulin A, Demidkina T Acta Crystallogr F Struct Biol Commun. 2016 Jan 1;72(Pt 1):65-71. doi:, 10.1107/S2053230X15023869. Epub 2016 Jan 1. PMID:26750487[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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