4hf8: Difference between revisions
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==Crystal structure of L-methionine gamma-lyase from Citrobacter freundii with glycine== | |||
<StructureSection load='4hf8' size='340' side='right' caption='[[4hf8]], [[Resolution|resolution]] 2.45Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4hf8]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HF8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HF8 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PLG:N-GLYCINE-[3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YL-METHANE]'>PLG</scene></td></tr> | |||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1y4i|1y4i]], [[2rfv|2rfv]], [[3jwa|3jwa]], [[3jwb|3jwb]], [[3jw9|3jw9]]</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methionine_gamma-lyase Methionine gamma-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.11 4.4.1.11] </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=4hf8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hf8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hf8 RCSB], [http://www.ebi.ac.uk/pdbsum/4hf8 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The three-dimensional structure of the external aldimine of Citrobacter freundii methionine gamma-lyase with competitive inhibitor glycine has been determined at 2.45 A resolution. It revealed subtle conformational changes providing effective binding of the inhibitor and facilitating labilization of Calpha-protons of the external aldimine. The structure shows that 1, 3-prototropic shift of Calpha-proton to C4'-atom of the cofactor may proceed with participation of active site Lys210 residue whose location is favorable for performing this transformation by a concerted mechanism. The observed stereoselectivity of isotopic exchange of enantiotopic Calpha-protons of glycine may be explained on the basis of external aldimine structure. The exchange of Calpha-pro-(R)-proton of the external aldimine might proceed in the course of the concerted transfer of the proton from Calpha-atom of glycine to C4'-atom of the cofactor. The exchange of Calpha-pro-(S)-proton may be performed with participation of Tyr113 residue which should be present in its basic form. The isotopic exchange of beta-protons, which is observed for amino acids bearing longer side groups, may be effected by two catalytic groups: Lys210 in its basic form, and Tyr113 acting as a general acid. | |||
Crystal structure of the external aldimine of Citrobacter freundii methionine gamma-lyase with glycine provides insight in mechanisms of two stages of physiological reaction and isotope exchange of alpha- and beta-protons of competitive inhibitors.,Revtovich SV, Faleev NG, Morozova EA, Anufrieva NV, Nikulin AD, Demidkina TV Biochimie. 2014 Jun;101:161-7. doi: 10.1016/j.biochi.2014.01.007. Epub 2014 Jan, 24. PMID:24463191<ref>PMID:24463191</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Methionine gamma-lyase]] | [[Category: Methionine gamma-lyase]] | ||
[[Category: Anufrieva, N V | [[Category: Anufrieva, N V]] | ||
[[Category: Demidkina, T V | [[Category: Demidkina, T V]] | ||
[[Category: Morozova, E A | [[Category: Morozova, E A]] | ||
[[Category: Nikulin, A D | [[Category: Nikulin, A D]] | ||
[[Category: Revtovich, S V | [[Category: Revtovich, S V]] | ||
[[Category: Complex]] | [[Category: Complex]] | ||
[[Category: L-methionine]] | [[Category: L-methionine]] | ||
Revision as of 10:35, 12 November 2014
Crystal structure of L-methionine gamma-lyase from Citrobacter freundii with glycineCrystal structure of L-methionine gamma-lyase from Citrobacter freundii with glycine
Structural highlights
Publication Abstract from PubMedThe three-dimensional structure of the external aldimine of Citrobacter freundii methionine gamma-lyase with competitive inhibitor glycine has been determined at 2.45 A resolution. It revealed subtle conformational changes providing effective binding of the inhibitor and facilitating labilization of Calpha-protons of the external aldimine. The structure shows that 1, 3-prototropic shift of Calpha-proton to C4'-atom of the cofactor may proceed with participation of active site Lys210 residue whose location is favorable for performing this transformation by a concerted mechanism. The observed stereoselectivity of isotopic exchange of enantiotopic Calpha-protons of glycine may be explained on the basis of external aldimine structure. The exchange of Calpha-pro-(R)-proton of the external aldimine might proceed in the course of the concerted transfer of the proton from Calpha-atom of glycine to C4'-atom of the cofactor. The exchange of Calpha-pro-(S)-proton may be performed with participation of Tyr113 residue which should be present in its basic form. The isotopic exchange of beta-protons, which is observed for amino acids bearing longer side groups, may be effected by two catalytic groups: Lys210 in its basic form, and Tyr113 acting as a general acid. Crystal structure of the external aldimine of Citrobacter freundii methionine gamma-lyase with glycine provides insight in mechanisms of two stages of physiological reaction and isotope exchange of alpha- and beta-protons of competitive inhibitors.,Revtovich SV, Faleev NG, Morozova EA, Anufrieva NV, Nikulin AD, Demidkina TV Biochimie. 2014 Jun;101:161-7. doi: 10.1016/j.biochi.2014.01.007. Epub 2014 Jan, 24. PMID:24463191[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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