This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


4mtu

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (12:29, 1 March 2024) (edit) (undo)
 
(3 intermediate revisions not shown.)
Line 1: Line 1:
 +
==beta-Alanyl-CoA:Ammonia Lyase from Clostridium propionicum==
==beta-Alanyl-CoA:Ammonia Lyase from Clostridium propionicum==
-
<StructureSection load='4mtu' size='340' side='right' caption='[[4mtu]], [[Resolution|resolution]] 0.97&Aring;' scene=''>
+
<StructureSection load='4mtu' size='340' side='right'caption='[[4mtu]], [[Resolution|resolution]] 0.97&Aring;' scene=''>
== Structural highlights ==
== 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>
+
<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"><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]] 0.97&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4mzq|4mzq]]</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'>[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>
+
<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>
-
<div style="background-color:#fffaf0;">
+
== Function ==
-
== Publication Abstract from PubMed ==
+
[https://www.uniprot.org/uniprot/Q6KC22_ANAPI Q6KC22_ANAPI]
-
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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
== References ==
+
-
<references/>
+
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Heine, A]]
+
[[Category: Anaerotignum propionicum]]
-
[[Category: Reuter, K]]
+
[[Category: Large Structures]]
-
[[Category: Hot dog fold]]
+
[[Category: Heine A]]
-
[[Category: Lyase]]
+
[[Category: Reuter K]]

Current revision

beta-Alanyl-CoA:Ammonia Lyase from Clostridium propionicum

PDB ID 4mtu

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4mtu"
Personal tools