Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
16
pubmed:dateCreated
1996-12-16
pubmed:abstractText
The three-dimensional structure of recombinant homodimeric delta9 stearoyl-acyl carrier protein desaturase, the archetype of the soluble plant fatty acid desaturases that convert saturated to unsaturated fatty acids, has been determined by protein crystallographic methods to a resolution of 2.4 angstroms. The structure was solved by a combination of single isomorphous replacement, anomalous contribution from the iron atoms to the native diffraction data and 6-fold non-crystallographic symmetry averaging. The 363 amino acid monomer consists of a single domain of 11 alpha-helices. Nine of these form an antiparallel helix bundle. The enzyme subunit contains a di-iron centre, with ligands from four of the alpha-helices in the helix bundle. The iron ions are bound in a highly symmetric environment, with one of the irons forming interactions with the side chains of E196 and H232 and the second iron with the side chains of E105 and H146. Two additional glutamic acid side chains, from E143 and E229, are within coordination distance to both iron ions. A water molecule is found within the second coordination sphere from the iron atoms. The lack of electron density corresponding to a mu-oxo bridge, and the long (4.2 angstroms) distance between the iron ions suggests that this probably represents the diferrous form of the enzyme. A deep channel which probably binds the fatty acid extends from the surface into the interior of the enzyme. Modelling of the substrate, stearic acid, into this channel places the delta9 carbon atom in the vicinity of one of the iron ions.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/8861937-1454797, http://linkedlifedata.com/resource/pubmed/commentcorrection/8861937-15299456, http://linkedlifedata.com/resource/pubmed/commentcorrection/8861937-1593637, http://linkedlifedata.com/resource/pubmed/commentcorrection/8861937-1644180, http://linkedlifedata.com/resource/pubmed/commentcorrection/8861937-17739077, http://linkedlifedata.com/resource/pubmed/commentcorrection/8861937-1978720, http://linkedlifedata.com/resource/pubmed/commentcorrection/8861937-2006187, http://linkedlifedata.com/resource/pubmed/commentcorrection/8861937-2006194, http://linkedlifedata.com/resource/pubmed/commentcorrection/8861937-2016748, http://linkedlifedata.com/resource/pubmed/commentcorrection/8861937-2025413, http://linkedlifedata.com/resource/pubmed/commentcorrection/8861937-2190093, http://linkedlifedata.com/resource/pubmed/commentcorrection/8861937-2428815, http://linkedlifedata.com/resource/pubmed/commentcorrection/8861937-2542262, http://linkedlifedata.com/resource/pubmed/commentcorrection/8861937-3681996, http://linkedlifedata.com/resource/pubmed/commentcorrection/8861937-4079774, http://linkedlifedata.com/resource/pubmed/commentcorrection/8861937-4300868, http://linkedlifedata.com/resource/pubmed/commentcorrection/8861937-4373719, http://linkedlifedata.com/resource/pubmed/commentcorrection/8861937-5945865, http://linkedlifedata.com/resource/pubmed/commentcorrection/8861937-6887253, http://linkedlifedata.com/resource/pubmed/commentcorrection/8861937-7118934, http://linkedlifedata.com/resource/pubmed/commentcorrection/8861937-7548115, http://linkedlifedata.com/resource/pubmed/commentcorrection/8861937-7640528, http://linkedlifedata.com/resource/pubmed/commentcorrection/8861937-7770774, http://linkedlifedata.com/resource/pubmed/commentcorrection/8861937-7947683, http://linkedlifedata.com/resource/pubmed/commentcorrection/8861937-7947684, http://linkedlifedata.com/resource/pubmed/commentcorrection/8861937-7961667, http://linkedlifedata.com/resource/pubmed/commentcorrection/8861937-7991701, http://linkedlifedata.com/resource/pubmed/commentcorrection/8861937-8255292, http://linkedlifedata.com/resource/pubmed/commentcorrection/8861937-8331655, http://linkedlifedata.com/resource/pubmed/commentcorrection/8861937-8395205, http://linkedlifedata.com/resource/pubmed/commentcorrection/8861937-8460163, http://linkedlifedata.com/resource/pubmed/commentcorrection/8861937-8550538, http://linkedlifedata.com/resource/pubmed/commentcorrection/8861937-8749363
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Fatty Acid Desaturases, http://linkedlifedata.com/resource/pubmed/chemical/Iron, http://linkedlifedata.com/resource/pubmed/chemical/Mixed Function Oxygenases, http://linkedlifedata.com/resource/pubmed/chemical/Oxygenases, http://linkedlifedata.com/resource/pubmed/chemical/Plant Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleotide Reductases, http://linkedlifedata.com/resource/pubmed/chemical/acyl-(acyl-carrier-protein)desaturas..., http://linkedlifedata.com/resource/pubmed/chemical/delta-9 fatty acid desaturase, http://linkedlifedata.com/resource/pubmed/chemical/methane monooxygenase
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0261-4189
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
15
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4081-92
pubmed:dateRevised
2010-9-10
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Crystal structure of delta9 stearoyl-acyl carrier protein desaturase from castor seed and its relationship to other di-iron proteins.
pubmed:affiliation
Department of Medical Biochemistry and Biophysics, Karolinska Institute, Stockholm, Sweden.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't