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5vj1

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Current revision (14:10, 13 March 2024) (edit) (undo)
 
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<StructureSection load='5vj1' size='340' side='right'caption='[[5vj1]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
<StructureSection load='5vj1' size='340' side='right'caption='[[5vj1]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5vj1]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VJ1 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5VJ1 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5vj1]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa], [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1] and [https://en.wikipedia.org/wiki/Pseudomonas_protegens_Pf-5 Pseudomonas protegens Pf-5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VJ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5VJ1 FirstGlance]. <br>
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</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=COA:COENZYME+A'>COA</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.995&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5vip|5vip]], [[5vit|5vit]]</td></tr>
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<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=COA:COENZYME+A'>COA</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Malonyl-S-ACP:biotin-protein_carboxyltransferase Malonyl-S-ACP:biotin-protein carboxyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.3.10 2.1.3.10] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5vj1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vj1 OCA], [https://pdbe.org/5vj1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5vj1 RCSB], [https://www.ebi.ac.uk/pdbsum/5vj1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5vj1 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5vj1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vj1 OCA], [http://pdbe.org/5vj1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5vj1 RCSB], [http://www.ebi.ac.uk/pdbsum/5vj1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5vj1 ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/MDCC_PSEF5 MDCC_PSEF5]] Subunit of malonate decarboxylase, it is an acyl carrier protein to which acetyl and malonyl thioester residues are bound via a 2'-(5''-phosphoribosyl)-3'-dephospho-CoA prosthetic group and turn over during the catalytic mechanism.
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[https://www.uniprot.org/uniprot/Q9I6T0_PSEAE Q9I6T0_PSEAE]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Pseudomonas species and other aerobic bacteria have a biotin-independent malonate decarboxylase that is crucial for their utilization of malonate as the sole carbon and energy source. The malonate decarboxylase holoenzyme contains four subunits, having an acyl-carrier protein (MdcC subunit) with a distinct prosthetic group, as well as decarboxylase (MdcD-MdcE) and acyl-carrier protein transferase (MdcA) catalytic activities. Here we report the crystal structure of a Pseudomonas malonate decarboxylase hetero-tetramer, as well as biochemical and functional studies based on the structural information. We observe a malonate molecule in the active site of MdcA and we also determine the structure of malonate decarboxylase with CoA in the active site of MdcD-MdcE. Both structures provide molecular insights into malonate decarboxylase catalysis. Mutations in the hetero-tetramer interface can abolish holoenzyme formation. Mutations in the hetero-tetramer interface and the active sites can abolish Pseudomonas aeruginosa growth in a defined medium with malonate as the sole carbon source.Some aerobic bacteria contain a biotin-independent malonate decarboxylase (MDC), which allows them to use malonate as the sole carbon source. Here, the authors present the crystal structure of a Pseudomonas MDC and give insights into its catalytic mechanism and function.
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Crystal structure of a Pseudomonas malonate decarboxylase holoenzyme hetero-tetramer.,Maderbocus R, Fields BL, Hamilton K, Luo S, Tran TH, Dietrich LEP, Tong L Nat Commun. 2017 Jul 31;8(1):160. doi: 10.1038/s41467-017-00233-z. PMID:28757619<ref>PMID:28757619</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5vj1" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Malonyl-S-ACP:biotin-protein carboxyltransferase]]
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[[Category: Pseudomonas aeruginosa]]
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[[Category: Maderbocus, R]]
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[[Category: Pseudomonas aeruginosa PAO1]]
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[[Category: Tong, L]]
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[[Category: Pseudomonas protegens Pf-5]]
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[[Category: Acetyl-coa carboxylase]]
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[[Category: Maderbocus R]]
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[[Category: Acp transferase]]
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[[Category: Tong L]]
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[[Category: Coa transferase]]
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[[Category: Transferase]]
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Current revision

Crystal structure of a Pseudomonas malonate decarboxylase hetero-tetramer in complex with coenzyme A

PDB ID 5vj1

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