4ien: Difference between revisions
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==Crystal Structure of Acyl-CoA Hydrolase from Neisseria meningitidis FAM18== | |||
=== | <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 [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> | |||
</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> | |||
<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='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://www.rcsb.org/pdb/explore.do?structureId=4ien RCSB], [http://www.ebi.ac.uk/pdbsum/4ien PDBsum]</span></td></tr> | |||
</table> | |||
<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> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Acyl-CoA hydrolase]] | [[Category: Acyl-CoA hydrolase]] | ||
[[Category: Neimf]] | [[Category: Neimf]] | ||
[[Category: Forwood, J K | [[Category: Forwood, J K]] | ||
[[Category: Khandokar, Y B | [[Category: Khandokar, Y B]] | ||
[[Category: Hot dog fold]] | [[Category: Hot dog fold]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
Revision as of 10:04, 20 January 2015
Crystal Structure of Acyl-CoA Hydrolase from Neisseria meningitidis FAM18
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