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| | <StructureSection load='5lnq' size='340' side='right'caption='[[5lnq]], [[Resolution|resolution]] 1.98Å' scene=''> | | <StructureSection load='5lnq' size='340' side='right'caption='[[5lnq]], [[Resolution|resolution]] 1.98Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5lnq]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Leime Leime]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LNQ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5LNQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5lnq]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Leishmania_mexicana Leishmania mexicana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LNQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LNQ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAA:ACETOACETYL-COENZYME+A'>CAA</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]] 1.98Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LMXM_23_0690 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5665 LEIME])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAA:ACETOACETYL-COENZYME+A'>CAA</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acetyl-CoA_C-acyltransferase Acetyl-CoA C-acyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.16 2.3.1.16] </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=5lnq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lnq OCA], [https://pdbe.org/5lnq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lnq RCSB], [https://www.ebi.ac.uk/pdbsum/5lnq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lnq ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5lnq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lnq OCA], [http://pdbe.org/5lnq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lnq RCSB], [http://www.ebi.ac.uk/pdbsum/5lnq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lnq ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/E9AW84_LEIMU E9AW84_LEIMU] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Acetyl-CoA C-acyltransferase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Leime]] | |
| - | [[Category: Harijan, R K]] | |
| - | [[Category: Kiema, T R]] | |
| - | [[Category: Wierenga, R K]] | |
| - | [[Category: Acetoacetyl-coa]] | |
| | [[Category: Leishmania mexicana]] | | [[Category: Leishmania mexicana]] |
| - | [[Category: Lipid metabolism]] | + | [[Category: Harijan RK]] |
| - | [[Category: Scp2-thiolase]] | + | [[Category: Kiema T-R]] |
| - | [[Category: Transferase]] | + | [[Category: Wierenga RK]] |
| Structural highlights
Function
E9AW84_LEIMU
Publication Abstract from PubMed
Structures of the C123A variant of the dimeric Leishmania mexicana SCP2-thiolase (type-2) (Lm-thiolase), complexed with acetyl-CoA and acetoacetyl-CoA, respectively, are reported. The catalytic site of thiolase contains two oxyanion holes, OAH1 and OAH2, which are important for catalysis. The two structures reveal for the first time the hydrogen bond interactions of the CoA-thioester oxygen atom of the substrate with the hydrogen bond donors of OAH1 of a CHH-thiolase. The amino acid sequence fingerprints ( C: xS, N: EAF, G H: P) of three catalytic loops identify the active site geometry of the well-studied CNH-thiolases, whereas SCP2-thiolases (type-1, type-2) are classified as CHH-thiolases, having as corresponding fingerprints C: xS, H: DCF and G H: P. In all thiolases, OAH2 is formed by the main chain NH groups of two catalytic loops. In the well-studied CNH-thiolases, OAH1 is formed by a water (of the Wat-Asn(NEAF) dyad) and NE2 (of the GHP-histidine). In the two described liganded Lm-thiolase structures, it is seen that in this CHH-thiolase, OAH1 is formed by NE2 of His338 (HDCF) and His388 (GHP). Analysis of the OAH1 hydrogen bond networks suggests that the GHP-histidine is doubly protonated and positively charged in these complexes, whereas the HDCF histidine is neutral and singly protonated.
Crystallographic substrate binding studies of Leishmania mexicana SCP2-thiolase (type-2): unique features of oxyanion hole-1.,Harijan RK, Kiema TR, Syed SM, Qadir I, Mazet M, Bringaud F, Michels PA, Wierenga RK Protein Eng Des Sel. 2017 Jan 5. doi: 10.1093/protein/gzw080. PMID:28062645[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Harijan RK, Kiema TR, Syed SM, Qadir I, Mazet M, Bringaud F, Michels PA, Wierenga RK. Crystallographic substrate binding studies of Leishmania mexicana SCP2-thiolase (type-2): unique features of oxyanion hole-1. Protein Eng Des Sel. 2017 Jan 5. doi: 10.1093/protein/gzw080. PMID:28062645 doi:http://dx.doi.org/10.1093/protein/gzw080
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