3glm

<table><tr><td colspan='2'>[[3glm]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacteroides_symbiosus"_stevens_1956 "bacteroides symbiosus" stevens 1956]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GLM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GLM FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=COO:CROTONYL+COENZYME+A'>COO</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3gf3|3gf3]], [[3gf7|3gf7]], [[3gma|3gma]]</div></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gcdA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1512 "Bacteroides symbiosus" Stevens 1956])</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glutaconyl-CoA_decarboxylase Glutaconyl-CoA decarboxylase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.70 4.1.1.70] </span></td></tr>

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== Publication Abstract from PubMed ==

Glutaconyl-CoA decarboxylase (Gcd) couples the biotin-dependent decarboxylation of glutaconyl-CoA with the generation of an electrochemical Na(+) gradient. Sequencing of the genes encoding all subunits of the Clostridium symbiosum decarboxylase membrane complex revealed that it comprises two distinct biotin carrier subunits, GcdC(1) and GcdC(2), which differ in the length of a central alanine- and proline-rich linker domain. Co-crystallization of the decarboxylase subunit GcdA with the substrate glutaconyl-CoA, the product crotonyl-CoA, and the substrate analogue glutaryl-CoA, respectively, resulted in a high resolution model for substrate binding and catalysis revealing remarkable structural changes upon substrate binding. Unlike the GcdA structure from Acidaminococcus fermentans, these data suggest that in intact Gcd complexes, GcdA is associated as a tetramer crisscrossed by a network of solvent-filled tunnels.

An asymmetric model for Na+-translocating glutaconyl-CoA decarboxylases.,Kress D, Brugel D, Schall I, Linder D, Buckel W, Essen LO J Biol Chem. 2009 Oct 9;284(41):28401-9. Epub 2009 Aug 4. PMID:19654317<ref>PMID:19654317</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 3glm" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Bacteroides symbiosus stevens 1956]]

[[Category: Glutaconyl-CoA decarboxylase]]

[[Category: Brugel, D]]

[[Category: Buckel, W]]

[[Category: Essen, L O]]

[[Category: Kress, D]]

[[Category: Sodium ion transport]]