1afr: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
No edit summary
No edit summary
 
(15 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1afr.gif|left|200px]]<br /><applet load="1afr" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1afr, resolution 2.4&Aring;" />
'''STEAROYL-ACYL CARRIER PROTEIN DESATURASE FROM CASTOR SEEDS'''<br />


==Overview==
==STEAROYL-ACYL CARRIER PROTEIN DESATURASE FROM CASTOR SEEDS==
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.
<StructureSection load='1afr' size='340' side='right'caption='[[1afr]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1afr]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Ricinus_communis Ricinus communis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AFR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AFR FirstGlance]. <br>
1AFR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Ricinus_communis Ricinus communis] with <scene name='pdbligand=FE2:'>FE2</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Acyl-[acyl-carrier-protein]_desaturase Acyl-[acyl-carrier-protein] desaturase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.19.2 1.14.19.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AFR OCA].
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene></td></tr>
==Reference==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1afr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1afr OCA], [https://pdbe.org/1afr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1afr RCSB], [https://www.ebi.ac.uk/pdbsum/1afr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1afr ProSAT]</span></td></tr>
Crystal structure of delta9 stearoyl-acyl carrier protein desaturase from castor seed and its relationship to other di-iron proteins., Lindqvist Y, Huang W, Schneider G, Shanklin J, EMBO J. 1996 Aug 15;15(16):4081-92. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8861937 8861937]
</table>
[[Category: Acyl-[acyl-carrier-protein] desaturase]]
== Function ==
[https://www.uniprot.org/uniprot/STAD_RICCO STAD_RICCO] Converts stearoyl-ACP to oleoyl-ACP by introduction of a cis double bond between carbons Delta(9) and Delta(10) of the acyl chain.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/af/1afr_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1afr ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Ricinus communis]]
[[Category: Ricinus communis]]
[[Category: Single protein]]
[[Category: Huang W]]
[[Category: Huang, W.]]
[[Category: Lindqvist Y]]
[[Category: Lindqvist, Y.]]
[[Category: Schneider G]]
[[Category: Schneider, G.]]
[[Category: FE2]]
[[Category: binuclear iron center]]
[[Category: electron transfer]]
[[Category: fatty acid biosynthesis]]
[[Category: fatty acid desaturase]]
[[Category: oxidoreductase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:44:00 2008''

Latest revision as of 09:30, 7 February 2024

STEAROYL-ACYL CARRIER PROTEIN DESATURASE FROM CASTOR SEEDSSTEAROYL-ACYL CARRIER PROTEIN DESATURASE FROM CASTOR SEEDS

Structural highlights

1afr is a 6 chain structure with sequence from Ricinus communis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.4Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

STAD_RICCO Converts stearoyl-ACP to oleoyl-ACP by introduction of a cis double bond between carbons Delta(9) and Delta(10) of the acyl chain.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

1afr, resolution 2.40Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=1afr&oldid=4040111"