4mtu
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4mtu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Anaerotignum_propionicum Anaerotignum 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 [https://proteopedia.org/fgij/fg.htm?mol=4MTU FirstGlance]. <br> | <table><tr><td colspan='2'>[[4mtu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Anaerotignum_propionicum Anaerotignum 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 [https://proteopedia.org/fgij/fg.htm?mol=4MTU FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 0.97Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4mtu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mtu OCA], [https://pdbe.org/4mtu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mtu RCSB], [https://www.ebi.ac.uk/pdbsum/4mtu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mtu ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4mtu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mtu OCA], [https://pdbe.org/4mtu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mtu RCSB], [https://www.ebi.ac.uk/pdbsum/4mtu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mtu ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/Q6KC22_ANAPI Q6KC22_ANAPI] | [https://www.uniprot.org/uniprot/Q6KC22_ANAPI Q6KC22_ANAPI] | ||
| - | <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. | ||
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| - | 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> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4mtu" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
beta-Alanyl-CoA:Ammonia Lyase from Clostridium propionicum
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