4ien: Difference between revisions
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== | ==Crystal Structure of Acyl-CoA Hydrolase from Neisseria meningitidis FAM18== | ||
[[4ien]] is a 4 chain structure with sequence from [ | <StructureSection load='4ien' size='340' side='right'caption='[[4ien]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | |||
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</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='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> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A1KUS8_NEIMF A1KUS8_NEIMF] | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:24192375</ref> | |||
<ref | |||
[[Category: | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
[[Category: | </div> | ||
[[Category: Forwood | <div class="pdbe-citations 4ien" style="background-color:#fffaf0;"></div> | ||
[[Category: Khandokar | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Neisseria meningitidis FAM18]] | |||
[[Category: Forwood JK]] | |||
[[Category: Khandokar YB]] | |||
Latest revision as of 14:14, 8 November 2023
Crystal Structure of Acyl-CoA Hydrolase from Neisseria meningitidis FAM18
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