5w7d: Difference between revisions

Revision as of 05:47, 3 January 2018

Murine acyloxyacyl hydrolase (AOAH), S262A mutant

Structural highlights

5w7d is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	CA, GOL, MYR, NAG, PX8
Activity:	Acyloxyacyl hydrolase, with EC number 3.1.1.77
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[AOAH_MOUSE] Removes the secondary (acyloxyacyl-linked) fatty acyl chains from the lipid A region of bacterial lipopolysaccharides (LPS) (PubMed:12810692, PubMed:15155618, PubMed:17322564, PubMed:19860560). By breaking down LPS, terminates the host response to bacterial infection and prevents prolonged and damaging inflammatory responses (PubMed:17322564, PubMed:19860560, PubMed:28622363). In peritoneal macrophages, seems to be important for recovery from a state of immune tolerance following infection by Gram-negative bacteria (PubMed:18779055).^[1] ^[2] ^[3] ^[4] ^[5] ^[6]

References

↑ Lu M, Zhang M, Kitchens RL, Fosmire S, Takashima A, Munford RS. Stimulus-dependent deacylation of bacterial lipopolysaccharide by dendritic cells. J Exp Med. 2003 Jun 16;197(12):1745-54. doi: 10.1084/jem.20030420. PMID:12810692 doi:https://dx.doi.org/10.1084/jem.20030420
↑ Feulner JA, Lu M, Shelton JM, Zhang M, Richardson JA, Munford RS. Identification of acyloxyacyl hydrolase, a lipopolysaccharide-detoxifying enzyme, in the murine urinary tract. Infect Immun. 2004 Jun;72(6):3171-8. doi: 10.1128/IAI.72.6.3171-3178.2004. PMID:15155618 doi:https://dx.doi.org/10.1128/IAI.72.6.3171-3178.2004
↑ Shao B, Lu M, Katz SC, Varley AW, Hardwick J, Rogers TE, Ojogun N, Rockey DC, Dematteo RP, Munford RS. A host lipase detoxifies bacterial lipopolysaccharides in the liver and spleen. J Biol Chem. 2007 May 4;282(18):13726-35. doi: 10.1074/jbc.M609462200. Epub 2007 , Feb 24. PMID:17322564 doi:https://dx.doi.org/10.1074/jbc.M609462200
↑ Lu M, Varley AW, Ohta S, Hardwick J, Munford RS. Host inactivation of bacterial lipopolysaccharide prevents prolonged tolerance following gram-negative bacterial infection. Cell Host Microbe. 2008 Sep 11;4(3):293-302. doi: 10.1016/j.chom.2008.06.009. PMID:18779055 doi:https://dx.doi.org/10.1016/j.chom.2008.06.009
↑ Ojogun N, Kuang TY, Shao B, Greaves DR, Munford RS, Varley AW. Overproduction of acyloxyacyl hydrolase by macrophages and dendritic cells prevents prolonged reactions to bacterial lipopolysaccharide in vivo. J Infect Dis. 2009 Dec 1;200(11):1685-93. doi: 10.1086/646616. PMID:19860560 doi:https://dx.doi.org/10.1086/646616
↑ Zou B, Jiang W, Han H, Li J, Mao W, Tang Z, Yang Q, Qian G, Qian J, Zeng W, Gu J, Chu T, Zhu N, Zhang W, Yan D, He R, Chu Y, Lu M. Acyloxyacyl hydrolase promotes the resolution of lipopolysaccharide-induced acute lung injury. PLoS Pathog. 2017 Jun 16;13(6):e1006436. doi: 10.1371/journal.ppat.1006436., eCollection 2017 Jun. PMID:28622363 doi:https://dx.doi.org/10.1371/journal.ppat.1006436

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OCA

[1] Lu M, Zhang M, Kitchens RL, Fosmire S, Takashima A, Munford RS. Stimulus-dependent deacylation of bacterial lipopolysaccharide by dendritic cells. J Exp Med. 2003 Jun 16;197(12):1745-54. doi: 10.1084/jem.20030420. PMID:12810692 doi:https://dx.doi.org/10.1084/jem.20030420

[2] Feulner JA, Lu M, Shelton JM, Zhang M, Richardson JA, Munford RS. Identification of acyloxyacyl hydrolase, a lipopolysaccharide-detoxifying enzyme, in the murine urinary tract. Infect Immun. 2004 Jun;72(6):3171-8. doi: 10.1128/IAI.72.6.3171-3178.2004. PMID:15155618 doi:https://dx.doi.org/10.1128/IAI.72.6.3171-3178.2004

[3] Shao B, Lu M, Katz SC, Varley AW, Hardwick J, Rogers TE, Ojogun N, Rockey DC, Dematteo RP, Munford RS. A host lipase detoxifies bacterial lipopolysaccharides in the liver and spleen. J Biol Chem. 2007 May 4;282(18):13726-35. doi: 10.1074/jbc.M609462200. Epub 2007 , Feb 24. PMID:17322564 doi:https://dx.doi.org/10.1074/jbc.M609462200

[4] Lu M, Varley AW, Ohta S, Hardwick J, Munford RS. Host inactivation of bacterial lipopolysaccharide prevents prolonged tolerance following gram-negative bacterial infection. Cell Host Microbe. 2008 Sep 11;4(3):293-302. doi: 10.1016/j.chom.2008.06.009. PMID:18779055 doi:https://dx.doi.org/10.1016/j.chom.2008.06.009

[5] Ojogun N, Kuang TY, Shao B, Greaves DR, Munford RS, Varley AW. Overproduction of acyloxyacyl hydrolase by macrophages and dendritic cells prevents prolonged reactions to bacterial lipopolysaccharide in vivo. J Infect Dis. 2009 Dec 1;200(11):1685-93. doi: 10.1086/646616. PMID:19860560 doi:https://dx.doi.org/10.1086/646616

[6] Zou B, Jiang W, Han H, Li J, Mao W, Tang Z, Yang Q, Qian G, Qian J, Zeng W, Gu J, Chu T, Zhu N, Zhang W, Yan D, He R, Chu Y, Lu M. Acyloxyacyl hydrolase promotes the resolution of lipopolysaccharide-induced acute lung injury. PLoS Pathog. 2017 Jun 16;13(6):e1006436. doi: 10.1371/journal.ppat.1006436., eCollection 2017 Jun. PMID:28622363 doi:https://dx.doi.org/10.1371/journal.ppat.1006436

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5w7d is ON HOLD  until Paper Publication
+==Murine acyloxyacyl hydrolase (AOAH), S262A mutant==
+<StructureSection load='5w7d' size='340' side='right' caption='[[5w7d]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
-Authors:
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5w7d]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5W7D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5W7D FirstGlance]. <br>
-Description:
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PX8:1,2-DISTEAROYL-SN-GLYCERO-3-PHOSPHATE'>PX8</scene></td></tr>
-[[Category: Unreleased Structures]]
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acyloxyacyl_hydrolase Acyloxyacyl hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.77 3.1.1.77] </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=5w7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5w7d OCA], [http://pdbe.org/5w7d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5w7d RCSB], [http://www.ebi.ac.uk/pdbsum/5w7d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5w7d ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/AOAH_MOUSE AOAH_MOUSE]] Removes the secondary (acyloxyacyl-linked) fatty acyl chains from the lipid A region of bacterial lipopolysaccharides (LPS) (PubMed:12810692, PubMed:15155618, PubMed:17322564, PubMed:19860560). By breaking down LPS, terminates the host response to bacterial infection and prevents prolonged and damaging inflammatory responses (PubMed:17322564, PubMed:19860560, PubMed:28622363). In peritoneal macrophages, seems to be important for recovery from a state of immune tolerance following infection by Gram-negative bacteria (PubMed:18779055).<ref>PMID:12810692</ref> <ref>PMID:15155618</ref> <ref>PMID:17322564</ref> <ref>PMID:18779055</ref> <ref>PMID:19860560</ref> <ref>PMID:28622363</ref>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Acyloxyacyl hydrolase]]
+[[Category: Gorelik, A]]
+[[Category: Illes, K]]
+[[Category: Nagar, B]]
+[[Category: Gdsl esterase]]
+[[Category: Hydrolase]]
+[[Category: Lipopolysaccharide]]
+[[Category: Lp]]
+[[Category: Saposin]]

5w7d: Difference between revisions

Revision as of 05:47, 3 January 2018

Murine acyloxyacyl hydrolase (AOAH), S262A mutant

Structural highlights

Function

References

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