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4g32

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Revision as of 21:46, 24 December 2014

Crystal Structure of a Phospholipid-Lipoxygenase Complex from Pseudomonas aeruginosa at 1.75A (P21212)

Structural highlights

4g32 is a 1 chain structure with sequence from "bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	4g33
Gene:	lox ("Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[LOX_PSEAI] In presence of oxygen, converts oleic acid into (S)-(E)-10-hydroperoxy-8-octadecenoic acid (HPOD), which spontaneously decomposes to the corresponding (E)-10-hydroxy-8-octadecenoic acid (HOD). In vivo, the reaction leads to the dihydroxy derivative (E)-7,10-dihydroxy-8-octadecenoic acid (DHOD), so that the three hydroxy-fatty acids can be isolated from the culture medium. Also active on linoleic acid and linolenic acid. Almost not active on arachidonic acid.

Publication Abstract from PubMed

Lipoxygenases (LOXs), which are essential in eukaryotes, have no confirmed function in prokaryotes that are devoid of polyunsaturated fatty acids. The structure of a secretable LOX from Pseudomonas aeruginosa (Pa_LOX), the first available from a prokaryote, presents significant differences with respect to eukaryotic LOXs, including a cluster of helices acting as a lid to the active center. The mobility of the lid and the structural variability of the N-terminal region of Pa_LOX was confirmed by comparing 2 crystal forms. The binding pocket contains a phosphatidylethanolamine phospholipid with branches of 18 (sn-1) and 14/16 (sn-2) carbon atoms in length. Carbon atoms from the sn-1 chain approach the catalytic iron in a manner that sheds light on how the enzymatic reaction might proceed. The findings in these studies suggest that Pa_LOX has the capacity to extract and modify unsaturated phospholipids from eukaryotic membranes, allowing this LOX to play a role in the interaction of P. aeruginosa with host cells.-Garreta, A., Val-Moraes, S. P., Garcia-Fernandez, Q., Montserrat Busquets, C. J., Oliver, A., Ortiz, A., Gaffney, B. J., Fita, I., Manresa, A., Carpena, X. Structure and interaction with phospholipids of a prokaryotic lipoxygenase from Pseudomonas aeruginosa.

Structure and interaction with phospholipids of a prokaryotic lipoxygenase from Pseudomonas aeruginosa.,Garreta A, Val-Moraes SP, Garcia-Fernandez Q, Busquets M, Juan C, Oliver A, Ortiz A, Gaffney BJ, Fita I, Manresa A, Carpena X FASEB J. 2013 Aug 30. PMID:23985801^[1]

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

References

↑ Garreta A, Val-Moraes SP, Garcia-Fernandez Q, Busquets M, Juan C, Oliver A, Ortiz A, Gaffney BJ, Fita I, Manresa A, Carpena X. Structure and interaction with phospholipids of a prokaryotic lipoxygenase from Pseudomonas aeruginosa. FASEB J. 2013 Aug 30. PMID:23985801 doi:http://dx.doi.org/10.1096/fj.13-235952

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4g32"

@@ Line 8: / Line 8: @@
 <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=4g32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g32 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4g32 RCSB], [http://www.ebi.ac.uk/pdbsum/4g32 PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/LOX_PSEAI LOX_PSEAI]] In presence of oxygen, converts oleic acid into (S)-(E)-10-hydroperoxy-8-octadecenoic acid (HPOD), which spontaneously decomposes to the corresponding (E)-10-hydroxy-8-octadecenoic acid (HOD). In vivo, the reaction leads to the dihydroxy derivative (E)-7,10-dihydroxy-8-octadecenoic acid (DHOD), so that the three hydroxy-fatty acids can be isolated from the culture medium. Also active on linoleic acid and linolenic acid. Almost not active on arachidonic acid.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

4g32

From Proteopedia

Revision as of 21:46, 24 December 2014

Crystal Structure of a Phospholipid-Lipoxygenase Complex from Pseudomonas aeruginosa at 1.75A (P21212)

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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