4mtu: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==beta-Alanyl-CoA:Ammonia Lyase from Clostridium propionicum== | |||
<StructureSection load='4mtu' size='340' side='right' caption='[[4mtu]], [[Resolution|resolution]] 0.97Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4mtu]] is a 1 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=4MTU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MTU FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br> | |||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4mzq|4mzq]]</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=4mtu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mtu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4mtu RCSB], [http://www.ebi.ac.uk/pdbsum/4mtu 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]] | ||
