2gej: Difference between revisions

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<StructureSection load='2gej' size='340' side='right'caption='[[2gej]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
<StructureSection load='2gej' size='340' side='right'caption='[[2gej]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2gej]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycs2 Mycs2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GEJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GEJ FirstGlance]. <br>
<table><tr><td colspan='2'>[[2gej]] 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=2GEJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GEJ FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDD:GUANOSINE-5-DIPHOSPHATE-ALPHA-D-MANNOSE'>GDD</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;'>[[2gek|2gek]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDD:GUANOSINE-5-DIPHOSPHATE-ALPHA-D-MANNOSE'>GDD</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PIMA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=246196 MYCS2])</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=2gej FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gej OCA], [https://pdbe.org/2gej PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gej RCSB], [https://www.ebi.ac.uk/pdbsum/2gej PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gej 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=2gej FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gej OCA], [https://pdbe.org/2gej PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gej RCSB], [https://www.ebi.ac.uk/pdbsum/2gej PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gej ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/PIMA_MYCS2 PIMA_MYCS2]] Catalyzes the addition of a mannose residue from GDP-D-mannose to the position 2 of a phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Contrary to PimB, the mannosyltransferase PimA is unable to transfer a mannose residue to the position 6 of the phosphatidyl-myo-inositola of PIM1.<ref>PMID:12068013</ref> <ref>PMID:19638342</ref>
[https://www.uniprot.org/uniprot/PIMA_MYCS2 PIMA_MYCS2] Catalyzes the addition of a mannose residue from GDP-D-mannose to the position 2 of a phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Contrary to PimB, the mannosyltransferase PimA is unable to transfer a mannose residue to the position 6 of the phosphatidyl-myo-inositola of PIM1.<ref>PMID:12068013</ref> <ref>PMID:19638342</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2gej ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2gej ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Mycobacterial phosphatidylinositol mannosides (PIMs) and metabolically derived cell wall lipoglycans play important roles in host-pathogen interactions, but their biosynthetic pathways are poorly understood. Here we focus on Mycobacterium smegmatis PimA, an essential enzyme responsible for the initial mannosylation of phosphatidylinositol. The structure of PimA in complex with GDP-mannose shows the two-domain organization and the catalytic machinery typical of GT-B glycosyltransferases. PimA is an amphitrophic enzyme that binds mono-disperse phosphatidylinositol, but its transferase activity is stimulated by high concentrations of non-substrate anionic surfactants, indicating that the early stages of PIM biosynthesis involve lipid-water interfacial catalysis. Based on structural, calorimetric, and mutagenesis studies, we propose a model wherein PimA attaches to the membrane through its N-terminal domain, and this association leads to enzyme activation. Our results reveal a novel mode of phosphatidylinositol recognition and provide a template for the development of potential antimycobacterial compounds.
Molecular recognition and interfacial catalysis by the essential phosphatidylinositol mannosyltransferase PimA from mycobacteria.,Guerin ME, Kordulakova J, Schaeffer F, Svetlikova Z, Buschiazzo A, Giganti D, Gicquel B, Mikusova K, Jackson M, Alzari PM J Biol Chem. 2007 Jul 13;282(28):20705-14. Epub 2007 May 16. PMID:17510062<ref>PMID:17510062</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2gej" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Mycs2]]
[[Category: Mycolicibacterium smegmatis MC2 155]]
[[Category: Alzari, P M]]
[[Category: Alzari PM]]
[[Category: Buschiazzo, A]]
[[Category: Buschiazzo A]]
[[Category: Guerin, M E]]
[[Category: Guerin ME]]
[[Category: Jackson, M]]
[[Category: Jackson M]]
[[Category: Kordulakova, J]]
[[Category: Kordulakova J]]
[[Category: Binary complex]]
[[Category: Gt4 glycosyltransferase]]
[[Category: Mannosyltransferase]]
[[Category: Rossmann fold]]
[[Category: Transferase]]

Latest revision as of 09:27, 14 February 2024

Crystal Structure of phosphatidylinositol mannosyltransferase (PimA) from Mycobacterium smegmatis in complex with GDP-Man

2gej, resolution 2.60Å

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