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5uzp

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Current revision (14:30, 6 March 2024) (edit) (undo)
 
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<StructureSection load='5uzp' size='340' side='right'caption='[[5uzp]], [[Resolution|resolution]] 2.29&Aring;' scene=''>
<StructureSection load='5uzp' size='340' side='right'caption='[[5uzp]], [[Resolution|resolution]] 2.29&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5uzp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UZP OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5UZP FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5uzp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UZP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5UZP 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=OAA:OXALOACETATE+ION'>OAA</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]] 2.29&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=OAA:OXALOACETATE+ION'>OAA</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/Citrate_(Si)-synthase Citrate (Si)-synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.3.1 2.3.3.1] </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=5uzp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uzp OCA], [https://pdbe.org/5uzp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5uzp RCSB], [https://www.ebi.ac.uk/pdbsum/5uzp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5uzp 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=5uzp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uzp OCA], [http://pdbe.org/5uzp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5uzp RCSB], [http://www.ebi.ac.uk/pdbsum/5uzp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5uzp ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/CISY_HUMAN CISY_HUMAN]
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Aspergillus fumigatus is a ubiquitous fungus that is not only a problem in agriculture, but also in healthcare. Aspergillus fumigatus drug resistance is becoming more prominent which is mainly attributed to the widespread use of fungicides in agriculture. The fungi-specific 2-methylcitrate cycle is responsible for detoxifying propionyl-CoA, a toxic metabolite produced as the fungus breaks down proteins and amino acids. The enzyme responsible for this detoxification is 2-methylcitrate synthase (mcsA) and is a potential candidate for the design of new anti-fungals. However, mcsA is very similar in structure to human citrate synthase (hCS) and catalyzes the same reaction. Therefore, both enzymes were studied in parallel to provide foundations for design of mcsA-specific inhibitors. The first crystal structures of citrate synthase from humans and 2-methylcitrate synthase from A. fumigatus are reported. The determined structures capture various conformational states of the enzymes and several inhibitors were identified and characterized. Despite a significant homology, mcsA and hCS display pronounced differences in substrate specificity and cooperativity. Considering that the active sites of the enzymes are almost identical, the differences in reactions catalyzed by enzymes are caused by residues that are in the vicinity of the active site and influence conformational changes of the enzymes.
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Comparative studies of Aspergillus fumigatus 2-methylcitrate synthase and human citrate synthase.,Schlachter CR, Klapper V, Radford T, Chruszcz M Biol Chem. 2019 Nov 26;400(12):1567-1581. doi: 10.1515/hsz-2019-0106. PMID:31141475<ref>PMID:31141475</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 5uzp" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Citrate Synthase 3D structures|Citrate Synthase 3D structures]]
*[[Citrate Synthase 3D structures|Citrate Synthase 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Chruszcz, M]]
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[[Category: Chruszcz M]]
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[[Category: Schlachter, C]]
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[[Category: Schlachter C]]
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[[Category: Transferase]]
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Current revision

Crystal structure of citrate synthase mutant A348G from homo sapiens

PDB ID 5uzp

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