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| | ==Crystal Structure of LpqW== | | ==Crystal Structure of LpqW== |
| - | <StructureSection load='2grv' size='340' side='right' caption='[[2grv]], [[Resolution|resolution]] 2.40Å' scene=''> | + | <StructureSection load='2grv' size='340' side='right'caption='[[2grv]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2grv]] is a 3 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=2GRV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2GRV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2grv]] is a 3 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=2GRV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GRV FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lpqW ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=246196 MYCS2])</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]] 2.4Å</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=2grv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2grv OCA], [http://pdbe.org/2grv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2grv RCSB], [http://www.ebi.ac.uk/pdbsum/2grv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2grv 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=2grv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2grv OCA], [https://pdbe.org/2grv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2grv RCSB], [https://www.ebi.ac.uk/pdbsum/2grv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2grv ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/LPQW_MYCS2 LPQW_MYCS2] May directly or indirectly regulate the accessibility of the key branch point intermediate, monoacyl phosphatidylinositol tetramannoside (AcPIM4), to the elongating alpha-1,6 mannosyltransferases which could regulate the lipoarabinomannans (LAMs) biosynthesis.<ref>PMID:18344361</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gr/2grv_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gr/2grv_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Mycs2]] | + | [[Category: Large Structures]] |
| - | [[Category: Marland, Z]] | + | [[Category: Mycolicibacterium smegmatis MC2 155]] |
| - | [[Category: Rossjohn, J]] | + | [[Category: Marland Z]] |
| - | [[Category: Biosynthetic protein]] | + | [[Category: Rossjohn J]] |
| - | [[Category: Substrate-binding protein scaffold]]
| + | |
| Structural highlights
Function
LPQW_MYCS2 May directly or indirectly regulate the accessibility of the key branch point intermediate, monoacyl phosphatidylinositol tetramannoside (AcPIM4), to the elongating alpha-1,6 mannosyltransferases which could regulate the lipoarabinomannans (LAMs) biosynthesis.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The waxy cell wall is crucial to the survival of mycobacteria within the infected host. The cell wall is a complex structure rich in unusual molecules that includes two related lipoglycans, the phosphatidylinositol mannosides (PIMs) and lipoarabinomannans (LAMs). Many proteins implicated in the PIM/LAM biosynthetic pathway, while attractive therapeutic targets, are poorly defined. The 2.4A resolution crystal structure of an essential lipoprotein, LpqW, implicated in LAM biosynthesis is reported here. LpqW adopts a scaffold reminiscent of the distantly related, promiscuous substrate-binding proteins of the ATP-binding cassette import system. Nevertheless, the unique closed conformation of LpqW suggests that mycobacteria and other closely related pathogens have hijacked this scaffold for use in key processes of cell wall biosynthesis. In silico docking provided a plausible model in which the candidate PIM ligand binds within a marked electronegative region located on the surface of LpqW. We suggest that LpqW represents an archetypal lipoprotein that channels intermediates from a pathway for mature PIM production into a pathway for LAM biosynthesis, thus controlling the relative abundance of these two important components of the cell wall.
Hijacking of a substrate-binding protein scaffold for use in mycobacterial cell wall biosynthesis.,Marland Z, Beddoe T, Zaker-Tabrizi L, Lucet IS, Brammananth R, Whisstock JC, Wilce MC, Coppel RL, Crellin PK, Rossjohn J J Mol Biol. 2006 Jun 16;359(4):983-97. Epub 2006 Apr 25. PMID:16698034[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Crellin PK, Kovacevic S, Martin KL, Brammananth R, Morita YS, Billman-Jacobe H, McConville MJ, Coppel RL. Mutations in pimE restore lipoarabinomannan synthesis and growth in a Mycobacterium smegmatis lpqW mutant. J Bacteriol. 2008 May;190(10):3690-9. PMID:18344361 doi:10.1128/JB.00200-08
- ↑ Marland Z, Beddoe T, Zaker-Tabrizi L, Lucet IS, Brammananth R, Whisstock JC, Wilce MC, Coppel RL, Crellin PK, Rossjohn J. Hijacking of a substrate-binding protein scaffold for use in mycobacterial cell wall biosynthesis. J Mol Biol. 2006 Jun 16;359(4):983-97. Epub 2006 Apr 25. PMID:16698034 doi:10.1016/j.jmb.2006.04.012
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