2r19

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Current revision (09:19, 21 February 2024) (edit) (undo)
 
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<StructureSection load='2r19' size='340' side='right'caption='[[2r19]], [[Resolution|resolution]] 2.16&Aring;' scene=''>
<StructureSection load='2r19' size='340' side='right'caption='[[2r19]], [[Resolution|resolution]] 2.16&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2r19]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2R19 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2R19 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2r19]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2R19 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2R19 FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2r1a|2r1a]]</div></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.16&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">yhbN, b3200, JW3167 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2r19 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r19 OCA], [https://pdbe.org/2r19 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2r19 RCSB], [https://www.ebi.ac.uk/pdbsum/2r19 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2r19 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=2r19 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r19 OCA], [https://pdbe.org/2r19 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2r19 RCSB], [https://www.ebi.ac.uk/pdbsum/2r19 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2r19 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/LPTA_ECOLI LPTA_ECOLI]] Involved in the assembly of lipopolysaccharide (LPS). Required for the translocation of LPS from the inner membrane to the outer membrane. May form a bridge between the inner membrane and the outer membrane, via interactions with LptC and LptD, thereby facilitating LPS transfer across the periplasm.[HAMAP-Rule:MF_01914]<ref>PMID:16765569</ref> <ref>PMID:17056748</ref> <ref>PMID:18424520</ref> <ref>PMID:18480051</ref> <ref>PMID:21169485</ref>
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[https://www.uniprot.org/uniprot/LPTA_ECOLI LPTA_ECOLI] Involved in the assembly of lipopolysaccharide (LPS). Required for the translocation of LPS from the inner membrane to the outer membrane. May form a bridge between the inner membrane and the outer membrane, via interactions with LptC and LptD, thereby facilitating LPS transfer across the periplasm.[HAMAP-Rule:MF_01914]<ref>PMID:16765569</ref> <ref>PMID:17056748</ref> <ref>PMID:18424520</ref> <ref>PMID:18480051</ref> <ref>PMID:21169485</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=2r19 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=2r19 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Lipopolysaccharide (LPS) transport protein A (LptA) is an essential periplasmic localized transport protein that has been implicated together with MsbA, LptB, and the Imp/RlpB complex in LPS transport from the inner membrane to the outer membrane, thereby contributing to building the cell envelope in Gram-negative bacteria and maintaining its integrity. Here we present the first crystal structures of processed Escherichia coli LptA in two crystal forms, one with two molecules in the asymmetric unit and the other with eight. In both crystal forms, severe anisotropic diffraction was corrected, which facilitated model building and structural refinement. The eight-molecule form of LptA is induced when LPS or Ra-LPS (a rough chemotype of LPS) is included during crystallization. The unique LptA structure represents a novel fold, consisting of 16 consecutive antiparallel beta-strands, folded to resemble a slightly twisted beta-jellyroll. Each LptA molecule interacts with an adjacent LptA molecule in a head-to-tail fashion to resemble long fibers. Site-directed mutagenesis of conserved residues located within a cluster that delineate the N-terminal beta-strands of LptA does not impair the function of the protein, although their overexpression appears more detrimental to LPS transport compared with wild-type LptA. Moreover, altered expression of both wild-type and mutated proteins interfered with normal LPS transport as witnessed by the production of an anomalous form of LPS. Structural analysis suggests that head-to-tail stacking of LptA molecules could be destabilized by the mutation, thereby potentially contributing to impair LPS transport.
 
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Novel structure of the conserved gram-negative lipopolysaccharide transport protein A and mutagenesis analysis.,Suits MD, Sperandeo P, Deho G, Polissi A, Jia Z J Mol Biol. 2008 Jul 11;380(3):476-88. Epub 2008 Apr 26. PMID:18534617<ref>PMID:18534617</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 2r19" style="background-color:#fffaf0;"></div>
 
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Ecoli]]
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[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Structural genomic]]
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[[Category: Jia Z]]
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[[Category: Jia, Z]]
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[[Category: Polissi A]]
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[[Category: Polissi, A]]
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[[Category: Suits MDL]]
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[[Category: Suits, M D.L]]
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[[Category: Beta-jellyroll]]
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[[Category: Beta-taco]]
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[[Category: Bsgi]]
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[[Category: Mainly beta]]
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[[Category: Transport protein]]
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Current revision

Crystal structure of the periplasmic lipopolysaccharide transport protein LptA (YhbN), orthorhombic form

PDB ID 2r19

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