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| | ==Crystal Structure of Acyl-CoA Hydrolase from Neisseria meningitidis FAM18== | | ==Crystal Structure of Acyl-CoA Hydrolase from Neisseria meningitidis FAM18== |
| - | <StructureSection load='4ien' size='340' side='right' caption='[[4ien]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='4ien' size='340' side='right'caption='[[4ien]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4ien]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Neimf Neimf]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IEN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4IEN FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4ien]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_meningitidis_FAM18 Neisseria meningitidis FAM18]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IEN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IEN FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene></td></tr> | + | </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>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NMC1417 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272831 NEIMF])</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=4ien FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ien OCA], [https://pdbe.org/4ien PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ien RCSB], [https://www.ebi.ac.uk/pdbsum/4ien PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ien ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acyl-CoA_hydrolase Acyl-CoA hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.2.20 3.1.2.20] </span></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=4ien FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ien OCA], [http://pdbe.org/4ien PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ien RCSB], [http://www.ebi.ac.uk/pdbsum/4ien PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ien ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A1KUS8_NEIMF A1KUS8_NEIMF] |
| | <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: Acyl-CoA hydrolase]] | + | [[Category: Large Structures]] |
| - | [[Category: Neimf]] | + | [[Category: Neisseria meningitidis FAM18]] |
| - | [[Category: Forwood, J K]] | + | [[Category: Forwood JK]] |
| - | [[Category: Khandokar, Y B]] | + | [[Category: Khandokar YB]] |
| - | [[Category: Hot dog fold]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
A1KUS8_NEIMF
Publication Abstract from PubMed
Neisseria meningitidis is the causative microorganism of many human diseases, including bacterial meningitis; together with Streptococcus pneumoniae, it accounts for approximately 80% of bacterial meningitis infections. The emergence of antibiotic-resistant strains of N. meningitidis has created a strong urgency for the development of new therapeutics, and the high-resolution structural elucidation of enzymes involved in cell metabolism represents a platform for drug development. Acetyl-CoA hydrolase is involved in multiple functions in the bacterial cell, including membrane synthesis, fatty-acid and lipid metabolism, gene regulation and signal transduction. Here, the first recombinant protein expression, purification and crystallization of a hexameric acetyl-CoA hydrolase from N. meningitidis are reported. This protein was crystallized using the hanging-drop vapour-diffusion technique at pH 8.5 and 290 K using ammonium phosphate as a precipitant. Optimized crystals diffracted to 2.0 A resolution at the Australian Synchrotron and belonged to space group P2(1)3 (unit-cell parameters a = b = c = 152.2 A), with four molecules in the asymmetric unit.
Expression, purification and crystallization of acetyl-CoA hydrolase from Neisseria meningitidis.,Khandokar YB, Londhe A, Patil S, Forwood JK Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Nov;69(Pt 11):1303-6. doi:, 10.1107/S1744309113028042. Epub 2013 Oct 30. PMID:24192375[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Khandokar YB, Londhe A, Patil S, Forwood JK. Expression, purification and crystallization of acetyl-CoA hydrolase from Neisseria meningitidis. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Nov;69(Pt 11):1303-6. doi:, 10.1107/S1744309113028042. Epub 2013 Oct 30. PMID:24192375 doi:http://dx.doi.org/10.1107/S1744309113028042
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