6bqc
From Proteopedia
(Difference between revisions)
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<StructureSection load='6bqc' size='340' side='right' caption='[[6bqc]], [[Resolution|resolution]] 2.07Å' scene=''> | <StructureSection load='6bqc' size='340' side='right' caption='[[6bqc]], [[Resolution|resolution]] 2.07Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6bqc]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BQC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BQC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6bqc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BQC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BQC FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=LOP:(1R)-2-{[(R)-(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}-1-[(DODECANOYLOXY)METHYL]ETHYL+(9Z)-OCTADEC-9-ENOATE'>LOP</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=LOP:(1R)-2-{[(R)-(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}-1-[(DODECANOYLOXY)METHYL]ETHYL+(9Z)-OCTADEC-9-ENOATE'>LOP</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cfa ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cyclopropane-fatty-acyl-phospholipid_synthase Cyclopropane-fatty-acyl-phospholipid synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.79 2.1.1.79] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cyclopropane-fatty-acyl-phospholipid_synthase Cyclopropane-fatty-acyl-phospholipid synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.79 2.1.1.79] </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=6bqc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bqc OCA], [http://pdbe.org/6bqc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bqc RCSB], [http://www.ebi.ac.uk/pdbsum/6bqc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bqc ProSAT]</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=6bqc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bqc OCA], [http://pdbe.org/6bqc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bqc RCSB], [http://www.ebi.ac.uk/pdbsum/6bqc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bqc ProSAT]</span></td></tr> | ||
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/CFA_ECOL6 CFA_ECOL6]] Transfers a methylene group from S-adenosyl-L-methionine to the cis double bond of an unsaturated fatty acid chain resulting in the replacement of the double bond with a methylene bridge. | [[http://www.uniprot.org/uniprot/CFA_ECOL6 CFA_ECOL6]] Transfers a methylene group from S-adenosyl-L-methionine to the cis double bond of an unsaturated fatty acid chain resulting in the replacement of the double bond with a methylene bridge. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Cell membranes must adapt to different environments. In Gram-negative bacteria, the inner membrane can be remodeled directly by modification of lipids embedded in the bilayer. For example, when Escherichia coli enters stationary phase, cyclopropane fatty acid (CFA) synthase converts most double bonds in unsaturated inner-membrane lipids into cyclopropyl groups. Here we report the crystal structure of E. coli CFA synthase. The enzyme is a dimer in the crystal and in solution, with each subunit containing a smaller N-domain that associates tightly with a larger catalytic C-domain, even following cleavage of the inter-domain linker or co-expression of each individual domain. Efficient catalysis requires dimerization and proper linkage of the two domains. These findings support an avidity-based model in which one subunit of the dimer stabilizes membrane binding, while the other subunit carries out catalysis. | ||
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| + | Structural and Functional Analysis of E. coli Cyclopropane Fatty Acid Synthase.,Hari SB, Grant RA, Sauer RT Structure. 2018 Jul 4. pii: S0969-2126(18)30214-4. doi:, 10.1016/j.str.2018.06.008. PMID:30057024<ref>PMID:30057024</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6bqc" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Bacillus coli migula 1895]] | ||
[[Category: Cyclopropane-fatty-acyl-phospholipid synthase]] | [[Category: Cyclopropane-fatty-acyl-phospholipid synthase]] | ||
[[Category: Grant, R A]] | [[Category: Grant, R A]] | ||
Revision as of 16:37, 15 August 2018
Cyclopropane fatty acid synthase from E. coli
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