1mm4: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
 
(One intermediate revision by the same user not shown)
Line 1: Line 1:


==Solution NMR structure of the outer membrane enzyme PagP in DPC micelles==
==Solution NMR structure of the outer membrane enzyme PagP in DPC micelles==
<StructureSection load='1mm4' size='340' side='right'caption='[[1mm4]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
<StructureSection load='1mm4' size='340' side='right'caption='[[1mm4]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1mm4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MM4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MM4 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1mm4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MM4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MM4 FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1mm5|1mm5]]</div></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CrcA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=1mm4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mm4 OCA], [https://pdbe.org/1mm4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mm4 RCSB], [https://www.ebi.ac.uk/pdbsum/1mm4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mm4 ProSAT]</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=1mm4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mm4 OCA], [https://pdbe.org/1mm4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mm4 RCSB], [https://www.ebi.ac.uk/pdbsum/1mm4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mm4 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/PAGP_ECOLI PAGP_ECOLI]] PagP is required both for biosynthesis of hepta-acylated lipid A species containing palmitate and for resistance to cationic antimicrobial peptides (CAMPs). It catalyzes the transfer of a palmitate chain (16:0) from the sn-1 position of a glycerophospholipid to the free hydroxyl group of the (R)-3-hydroxymyristate chain at position 2 of lipid A (endotoxin). Modifications of lipid A with a palmitate chain allow to evade host immune defenses by resisting antimicrobial peptides and attenuating the inflammatory response to infection triggered by lipopolysaccharide through the Toll-like receptor 4 (TLR4) signal transduction pathway. Phosphatidylglycerol (PtdGro), phosphatidylethanolamine (PtdEtn), phosphatidylserine (PtdSer) and phosphatidic acid (Ptd-OH) are all effective acyl donors.<ref>PMID:11013210</ref>
[https://www.uniprot.org/uniprot/PAGP_ECOLI PAGP_ECOLI] PagP is required both for biosynthesis of hepta-acylated lipid A species containing palmitate and for resistance to cationic antimicrobial peptides (CAMPs). It catalyzes the transfer of a palmitate chain (16:0) from the sn-1 position of a glycerophospholipid to the free hydroxyl group of the (R)-3-hydroxymyristate chain at position 2 of lipid A (endotoxin). Modifications of lipid A with a palmitate chain allow to evade host immune defenses by resisting antimicrobial peptides and attenuating the inflammatory response to infection triggered by lipopolysaccharide through the Toll-like receptor 4 (TLR4) signal transduction pathway. Phosphatidylglycerol (PtdGro), phosphatidylethanolamine (PtdEtn), phosphatidylserine (PtdSer) and phosphatidic acid (Ptd-OH) are all effective acyl donors.<ref>PMID:11013210</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 33: Line 32:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus coli migula 1895]]
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Bishop, R E]]
[[Category: Bishop RE]]
[[Category: Chen, L]]
[[Category: Chen L]]
[[Category: Choy, W Y]]
[[Category: Choy W-Y]]
[[Category: Forman-Kay, J D]]
[[Category: Forman-Kay JD]]
[[Category: Hwang, P M]]
[[Category: Hwang PM]]
[[Category: Kay, L E]]
[[Category: Kay LE]]
[[Category: Lo, E I]]
[[Category: Lo EI]]
[[Category: Prive, G G]]
[[Category: Prive GG]]
[[Category: Raetz, C R.H]]
[[Category: Raetz CRH]]
[[Category: Beta barrel]]
[[Category: Palmitoyltransferase]]
[[Category: Transferase]]
Retrieved from "https://proteopedia.org/1mm4"