3dbm

From Proteopedia

(Difference between revisions)

Current revision

Crystal Structure of Allene oxide synthase

Structural highlights

3dbm is a 1 chain structure with sequence from Parthenium argentatum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.6Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

C74A2_PARAR Involved in the biosynthesis of jasmonic acid, a growth regulator that is implicated also as a signaling molecule in plant defense. Acts on a number of unsaturated fatty-acid hydroperoxides, forming the corresponding allene oxides (By similarity).

Evolutionary Conservation

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

Publication Abstract from PubMed

Cytochrome P450s exist ubiquitously in all organisms and are involved in many biological processes. Allene oxide synthase (AOS) is a P450 enzyme that plays a key role in the biosynthesis of oxylipin jasmonates, which are involved in signal and defense reactions in higher plants. The crystal structures of guayule (Parthenium argentatum) AOS (CYP74A2) and its complex with the substrate analog 13(S)-hydroxyoctadeca-9Z,11E-dienoic acid have been determined. The structures exhibit a classic P450 fold but possess a heme-binding mode with an unusually long heme binding loop and a unique I-helix. The structures also reveal two channels through which substrate and product may access and leave the active site. The entrances are defined by a loop between beta3-2 and beta3-3. Asn-276 in the substrate binding site may interact with the substrate's hydroperoxy group and play an important role in catalysis, and Lys-282 at the entrance may control substrate access and binding. These studies provide both structural insights into AOS and related P450s and a structural basis to understand the distinct reaction mechanism.

Modes of heme binding and substrate access for cytochrome P450 CYP74A revealed by crystal structures of allene oxide synthase.,Li L, Chang Z, Pan Z, Fu ZQ, Wang X Proc Natl Acad Sci U S A. 2008 Sep 16;105(37):13883-8. Epub 2008 Sep 11. PMID:18787124^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Li L, Chang Z, Pan Z, Fu ZQ, Wang X. Modes of heme binding and substrate access for cytochrome P450 CYP74A revealed by crystal structures of allene oxide synthase. Proc Natl Acad Sci U S A. 2008 Sep 16;105(37):13883-8. Epub 2008 Sep 11. PMID:18787124

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3dbm"

Categories: Large Structures | Parthenium argentatum | Li L | Wang X

@@ Line 3: / Line 3: @@
 <StructureSection load='3dbm' size='340' side='right'caption='[[3dbm]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3dbm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Guayule_rubber_plant Guayule rubber plant]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DBM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DBM FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3dbm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Parthenium_argentatum Parthenium argentatum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DBM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DBM FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=HO2:(9E,11E,13S)-13-HYDROXYOCTADECA-9,11-DIENOIC+ACID'>HO2</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3dam|3dam]], [[3dan|3dan]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=HO2:(9E,11E,13S)-13-HYDROXYOCTADECA-9,11-DIENOIC+ACID'>HO2</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CYP74A2, RPP30 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=35935 Guayule rubber plant])</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Hydroperoxide_dehydratase Hydroperoxide dehydratase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.92 4.2.1.92] </span></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=3dbm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dbm OCA], [https://pdbe.org/3dbm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dbm RCSB], [https://www.ebi.ac.uk/pdbsum/3dbm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dbm ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/C74A2_PARAR C74A2_PARAR]] Involved in the biosynthesis of jasmonic acid, a growth regulator that is implicated also as a signaling molecule in plant defense. Acts on a number of unsaturated fatty-acid hydroperoxides, forming the corresponding allene oxides (By similarity).
+[https://www.uniprot.org/uniprot/C74A2_PARAR C74A2_PARAR] Involved in the biosynthesis of jasmonic acid, a growth regulator that is implicated also as a signaling molecule in plant defense. Acts on a number of unsaturated fatty-acid hydroperoxides, forming the corresponding allene oxides (By similarity).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 38: / Line 36: @@
 __TOC__
 </StructureSection>
-[[Category: Guayule rubber plant]]
-[[Category: Hydroperoxide dehydratase]]
 [[Category: Large Structures]]
-[[Category: Li, L]]
+[[Category: Parthenium argentatum]]
-[[Category: Wang, X]]
+[[Category: Li L]]
-[[Category: Crystal structure hem hode ao]]
+[[Category: Wang X]]
-[[Category: Fatty acid biosynthesis]]
-[[Category: Heme]]
-[[Category: Iron]]
-[[Category: Lipid synthesis]]
-[[Category: Lyase]]
-[[Category: Metal-binding]]
-[[Category: Oxylipin biosynthesis]]

3dbm

From Proteopedia

Current revision

Crystal Structure of Allene oxide synthase

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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