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5f31

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Current revision

Crystal structure of membrane associated PatA from Mycobacterium smegmatis in complex with palmitate - P 42 21 2 space group

Structural highlights

5f31 is a 1 chain structure with sequence from Mycolicibacterium smegmatis MC2 155. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.43Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ACYLT_MYCS2 Catalyzes the acylation to the position 6 of the alpha-1,2-linked mannose residue of the phosphatidyl-myo-inositol dimannoside (PIM2) or monomannoside (PIM1).^[1]

Publication Abstract from PubMed

The biosynthesis of phospholipids and glycolipids are critical pathways for virtually all cell membranes. PatA is an essential membrane associated acyltransferase involved in the biosynthesis of mycobacterial phosphatidyl-myo-inositol mannosides (PIMs). The enzyme transfers a palmitoyl moiety from palmitoyl-CoA to the 6-position of the mannose ring linked to 2-position of inositol in PIM1/PIM2. We report here the crystal structures of PatA from Mycobacterium smegmatis in the presence of its naturally occurring acyl donor palmitate and a nonhydrolyzable palmitoyl-CoA analog. The structures reveal an alpha/beta architecture, with the acyl chain deeply buried into a hydrophobic pocket that runs perpendicular to a long groove where the active site is located. Enzyme catalysis is mediated by an unprecedented charge relay system, which markedly diverges from the canonical HX4D motif. Our studies establish the mechanistic basis of substrate/membrane recognition and catalysis for an important family of acyltransferases, providing exciting possibilities for inhibitor design.

Structural basis for selective recognition of acyl chains by the membrane-associated acyltransferase PatA.,Albesa-Jove D, Svetlikova Z, Tersa M, Sancho-Vaello E, Carreras-Gonzalez A, Bonnet P, Arrasate P, Eguskiza A, Angala SK, Cifuente JO, Kordulakova J, Jackson M, Mikusova K, Guerin ME Nat Commun. 2016 Mar 11;7:10906. doi: 10.1038/ncomms10906. PMID:26965057^[2]

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

References

↑ Kordulakova J, Gilleron M, Puzo G, Brennan PJ, Gicquel B, Mikusova K, Jackson M. Identification of the required acyltransferase step in the biosynthesis of the phosphatidylinositol mannosides of mycobacterium species. J Biol Chem. 2003 Sep 19;278(38):36285-95. Epub 2003 Jul 8. PMID:12851411 doi:http://dx.doi.org/10.1074/jbc.M303639200
↑ Albesa-Jove D, Svetlikova Z, Tersa M, Sancho-Vaello E, Carreras-Gonzalez A, Bonnet P, Arrasate P, Eguskiza A, Angala SK, Cifuente JO, Kordulakova J, Jackson M, Mikusova K, Guerin ME. Structural basis for selective recognition of acyl chains by the membrane-associated acyltransferase PatA. Nat Commun. 2016 Mar 11;7:10906. doi: 10.1038/ncomms10906. PMID:26965057 doi:http://dx.doi.org/10.1038/ncomms10906

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/5f31"

@@ Line 3: / Line 3: @@
 <StructureSection load='5f31' size='340' side='right'caption='[[5f31]], [[Resolution|resolution]] 2.43&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5f31]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycs2 Mycs2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F31 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5F31 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5f31]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycolicibacterium_smegmatis_MC2_155 Mycolicibacterium smegmatis MC2 155]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F31 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5F31 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EOH:ETHANOL'>EOH</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</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]] 2.43&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MSMEG_2934, MSMEI_2860 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=246196 MYCS2])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EOH:ETHANOL'>EOH</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5f31 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f31 OCA], [http://pdbe.org/5f31 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5f31 RCSB], [http://www.ebi.ac.uk/pdbsum/5f31 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5f31 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=5f31 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f31 OCA], [https://pdbe.org/5f31 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5f31 RCSB], [https://www.ebi.ac.uk/pdbsum/5f31 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5f31 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/ACYLT_MYCS2 ACYLT_MYCS2]] Catalyzes the acylation to the position 6 of the alpha-1,2-linked mannose residue of the phosphatidyl-myo-inositol dimannoside (PIM2) or monomannoside (PIM1).<ref>PMID:12851411</ref>
+[https://www.uniprot.org/uniprot/ACYLT_MYCS2 ACYLT_MYCS2] Catalyzes the acylation to the position 6 of the alpha-1,2-linked mannose residue of the phosphatidyl-myo-inositol dimannoside (PIM2) or monomannoside (PIM1).<ref>PMID:12851411</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 24: / Line 24: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Mycs2]]
+[[Category: Mycolicibacterium smegmatis MC2 155]]
-[[Category: Albesa-Jove, D]]
+[[Category: Albesa-Jove D]]
-[[Category: Carreras-Gonzalez, A]]
+[[Category: Carreras-Gonzalez A]]
-[[Category: Cifuente, J O]]
+[[Category: Cifuente JO]]
-[[Category: Guerin, M E]]
+[[Category: Guerin ME]]
-[[Category: Mikusova, K]]
+[[Category: Mikusova K]]
-[[Category: Sancho-Vaello, E]]
+[[Category: Sancho-Vaello E]]
-[[Category: Svetlikova, Z]]
+[[Category: Svetlikova Z]]
-[[Category: Tersa, M]]
+[[Category: Tersa M]]
-[[Category: Acyltransferase]]
-[[Category: Glycolipid biosynthesis]]
-[[Category: Transferase]]

5f31

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Current revision

Crystal structure of membrane associated PatA from Mycobacterium smegmatis in complex with palmitate - P 42 21 2 space group

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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