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| | ==Crystal structure of N-terminal 618-residue fragment of LepB from Legionella pneumophila== | | ==Crystal structure of N-terminal 618-residue fragment of LepB from Legionella pneumophila== |
| - | <StructureSection load='4jw1' size='340' side='right' caption='[[4jw1]], [[Resolution|resolution]] 3.16Å' scene=''> | + | <StructureSection load='4jw1' size='340' side='right'caption='[[4jw1]], [[Resolution|resolution]] 3.16Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4jw1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_33152 Atcc 33152]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JW1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4JW1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4jw1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Legionella_pneumophila Legionella pneumophila]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JW1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JW1 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=4jw1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jw1 OCA], [https://pdbe.org/4jw1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jw1 RCSB], [https://www.ebi.ac.uk/pdbsum/4jw1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jw1 ProSAT]</span></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4jvs|4jvs]]</td></tr>
| + | |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lepB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=446 ATCC 33152])</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=4jw1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jw1 OCA], [http://pdbe.org/4jw1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4jw1 RCSB], [http://www.ebi.ac.uk/pdbsum/4jw1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4jw1 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q6X1Y7_LEGPN Q6X1Y7_LEGPN] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 33152]] | + | [[Category: Large Structures]] |
| - | [[Category: Hu, L]] | + | [[Category: Legionella pneumophila]] |
| - | [[Category: Shao, F]] | + | [[Category: Hu L]] |
| - | [[Category: Yao, Q]] | + | [[Category: Shao F]] |
| - | [[Category: Zhu, Y]] | + | [[Category: Yao Q]] |
| - | [[Category: Gtpase-accelerating protein]]
| + | [[Category: Zhu Y]] |
| - | [[Category: Hydrolase activator]]
| + | |
| - | [[Category: New gap fold]]
| + | |
| - | [[Category: Rab1]]
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| Structural highlights
Function
Q6X1Y7_LEGPN
Publication Abstract from PubMed
Rab GTPases are emerging targets of diverse bacterial pathogens. Here, we perform biochemical and structural analyses of LepB, a Rab GTPase-activating protein (GAP) effector from Legionella pneumophila. We map LepB GAP domain to residues 313-618 and show that the GAP domain is Rab1 specific with a catalytic activity higher than the canonical eukaryotic TBC GAP and the newly identified VirA/EspG family of bacterial RabGAP effectors. Exhaustive mutation analyses identify Arg444 as the arginine finger, but no catalytically essential glutamine residues. Crystal structures of LepB313-618 alone and the GAP domain of Legionella drancourtii LepB in complex with Rab1-GDP-AlF3 support the catalytic role of Arg444, and also further reveal a 3D architecture and a GTPase-binding mode distinct from all known GAPs. Glu449, structurally equivalent to TBC RabGAP glutamine finger in apo-LepB, undergoes a drastic movement upon Rab1 binding, which induces Rab1 Gln70 side-chain flipping towards GDP-AlF3 through a strong ionic interaction. This conformationally rearranged Gln70 acts as the catalytic cis-glutamine, therefore uncovering an unexpected RasGAP-like catalytic mechanism for LepB. Our studies highlight an extraordinary structural and catalytic diversity of RabGAPs, particularly those from bacterial pathogens.Cell Research advance online publication 16 April 2013; doi:10.1038/cr.2013.54.
Structural analyses of Legionella LepB reveal a new GAP fold that catalytically mimics eukaryotic RasGAP.,Yu Q, Hu L, Yao Q, Zhu Y, Dong N, Wang DC, Shao F Cell Res. 2013 Apr 16. doi: 10.1038/cr.2013.54. PMID:23588383[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Yu Q, Hu L, Yao Q, Zhu Y, Dong N, Wang DC, Shao F. Structural analyses of Legionella LepB reveal a new GAP fold that catalytically mimics eukaryotic RasGAP. Cell Res. 2013 Apr 16. doi: 10.1038/cr.2013.54. PMID:23588383 doi:10.1038/cr.2013.54
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