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5ugr
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Malyl-CoA lyase from Methylobacterium extorquens== | |
| + | <StructureSection load='5ugr' size='340' side='right' caption='[[5ugr]], [[Resolution|resolution]] 1.56Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5ugr]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UGR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UGR FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Malyl-CoA_lyase Malyl-CoA lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.3.24 4.1.3.24] </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=5ugr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ugr OCA], [http://pdbe.org/5ugr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ugr RCSB], [http://www.ebi.ac.uk/pdbsum/5ugr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ugr ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Malyl-CoA lyase (MCL) is an Mg2+-dependent enzyme that catalyzes the reversible cleavage of (2S)-4-malyl-CoA to yield acetyl-CoA and glyoxylate. MCL enzymes, which are found in a variety of bacteria, are members of the citrate lyase-like family and are involved in the assimilation of one- and two-carbon compounds. Here, the 1.56 A resolution X-ray crystal structure of MCL from Methylobacterium extorquens AM1 with bound Mg2+ is presented. Structural alignment with the closely related Rhodobacter sphaeroides malyl-CoA lyase complexed with Mg2+, oxalate and CoA allows a detailed analysis of the domain motion of the enzyme caused by substrate binding. Alignment of the structures shows that a simple hinge motion centered on the conserved residues Phe268 and Thr269 moves the C-terminal domain by about 30 degrees relative to the rest of the molecule. This domain motion positions a conserved aspartate residue located in the C-terminal domain in the active site of the adjacent monomer, which may serve as a general acid/base in the catalytic mechanism. | ||
| - | + | Structure of Methylobacterium extorquens malyl-CoA lyase: CoA-substrate binding correlates with domain shift.,Gonzalez JM, Marti-Arbona R, Chen JC, Unkefer CJ Acta Crystallogr F Struct Biol Commun. 2017 Feb 1;73(Pt 2):79-85. doi:, 10.1107/S2053230X17001029. Epub 2017 Jan 27. PMID:28177317<ref>PMID:28177317</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Gonzalez, J | + | <div class="pdbe-citations 5ugr" style="background-color:#fffaf0;"></div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Malyl-CoA lyase]] | ||
| + | [[Category: Gonzalez, J M]] | ||
| + | [[Category: Lyase]] | ||
Revision as of 06:36, 9 March 2017
Malyl-CoA lyase from Methylobacterium extorquens
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