4u2h: Difference between revisions
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==The crystal structure of apo CalE6, a methionine gamma lyase from Micromonospora echinospora== | ==The crystal structure of apo CalE6, a methionine gamma lyase from Micromonospora echinospora== | ||
<StructureSection load='4u2h' size='340' side='right' caption='[[4u2h]], [[Resolution|resolution]] 1.85Å' scene=''> | <StructureSection load='4u2h' size='340' side='right' caption='[[4u2h]], [[Resolution|resolution]] 1.85Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4u1t|4u1t]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4u1t|4u1t]]</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='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=4u2h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u2h OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4u2h RCSB], [http://www.ebi.ac.uk/pdbsum/4u2h 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=4u2h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u2h OCA], [http://pdbe.org/4u2h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4u2h RCSB], [http://www.ebi.ac.uk/pdbsum/4u2h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4u2h ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4u2h" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 20:33, 11 August 2016
The crystal structure of apo CalE6, a methionine gamma lyase from Micromonospora echinosporaThe crystal structure of apo CalE6, a methionine gamma lyase from Micromonospora echinospora
Structural highlights
Publication Abstract from PubMedCalE6 is a previously uncharacterized protein involved in the biosynthesis of calicheamicins in Micromonospora echinospora. It is a pyridoxal-5'-phosphate-dependent enzyme and exhibits high sequence homology to cystathionine gamma-lyases and cystathionine gamma-synthases. However, it was found to be active towards methionine and to convert this amino acid into alpha-ketobutyrate, ammonium, and methanethiol. The crystal structure of the cofactor-bound holoenzyme was resolved at 2.0 A; it contains two active site residues, Gly105 and Val322, specific for methionine gamma-lyases. Modeling of methionine into the active site allows identification of the active site residues responsible for substrate recognition and catalysis. These findings support that CalE6 is a putative methionine gamma-lyase producing methanethiol as a building block in biosynthesis of calicheamicins. Identification and Characterization of a Methionine gamma-Lyase in the Calicheamicin Biosynthetic Cluster of Micromonospora echinospora.,Song H, Xu R, Guo Z Chembiochem. 2015 Jan 2;16(1):100-9. doi: 10.1002/cbic.201402489. Epub 2014 Nov, 17. PMID:25404066[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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