5dx5: Difference between revisions
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5dx5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dx5 OCA], [http://pdbe.org/5dx5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dx5 RCSB], [http://www.ebi.ac.uk/pdbsum/5dx5 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5dx5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dx5 OCA], [http://pdbe.org/5dx5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dx5 RCSB], [http://www.ebi.ac.uk/pdbsum/5dx5 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
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== Publication Abstract from PubMed == | |||
Methionine 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<ref>PMID:26750487</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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<div class="pdbe-citations 5dx5" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 11:44, 20 January 2016
Crystal structure of methionine gamma-lyase from Clostridium sporogenesCrystal structure of methionine gamma-lyase from Clostridium sporogenes
Structural highlights
Publication 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. References
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