4mzq
From Proteopedia
(Difference between revisions)
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| - | + | ==beta-Alanyl-CoA:Ammonia Lyase from Clostridium propionicum in complex with propionyl-CoA== | |
| - | + | <StructureSection load='4mzq' size='340' side='right' caption='[[4mzq]], [[Resolution|resolution]] 1.59Å' scene=''> | |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4mzq]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/[clostridium]_propionicum [clostridium] propionicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MZQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MZQ FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1VU:PROPIONYL+COENZYME+A'>1VU</scene><br> | ||
| + | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4mtu|4mtu]]</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4mzq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mzq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4mzq RCSB], [http://www.ebi.ac.uk/pdbsum/4mzq PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Clostridium propionicum is the only organism known to ferment beta-alanine, a constituent of coenzyme A (CoA) and the phosphopantetheinyl prosthetic group of holo-acyl carrier protein. The first step in the fermentation is a CoA-transfer to beta-alanine. Subsequently, the resulting beta-alanyl-CoA is deaminated by the enzyme beta-alanyl-CoA:ammonia lyase (Acl) to reversibly form ammonia and acrylyl-CoA. We have determined the crystal structure of Acl in its apo-form at a resolution of 0.97 A as well as in complex with CoA at a resolution of 1.59 A. The structures reveal that the enyzme belongs to a superfamily of proteins exhibiting a so called "hot dog fold" which is characterized by a five-stranded antiparallel beta-sheet with a long alpha-helix packed against it. The functional unit of all "hot dog fold" proteins is a homodimer containing two equivalent substrate binding sites which are established by the dimer interface. In the case of Acl, three functional dimers combine to a homohexamer strongly resembling the homohexamer formed by YciA-like acyl-CoA thioesterases. Here, we propose an enzymatic mechanism based on the crystal structure of the Acl.CoA complex and molecular docking. Proteins 2014. (c) 2014 Wiley Periodicals, Inc. | ||
| - | + | High resolution crystal structure of Clostridium propionicum beta-alanyl-CoA:ammonia lyase, a new member of the "hot dog fold" protein superfamily.,Heine A, Herrmann G, Selmer T, Terwesten F, Buckel W, Reuter K Proteins. 2014 Mar 13. doi: 10.1002/prot.24557. PMID:24623648<ref>PMID:24623648</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Heine, A.]] | [[Category: Heine, A.]] | ||
[[Category: Reuter, K.]] | [[Category: Reuter, K.]] | ||
[[Category: Hot dog fold]] | [[Category: Hot dog fold]] | ||
[[Category: Lyase]] | [[Category: Lyase]] | ||
Revision as of 07:06, 11 June 2014
beta-Alanyl-CoA:Ammonia Lyase from Clostridium propionicum in complex with propionyl-CoA
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