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==Globular Domain Protein B Mycoplasma Pneumoniae complexed with 6'SL==
==N-Domain P40/P90 Mycoplasma pneumoniae complexed with 6'SL==
<StructureSection load='6tm0' size='340' side='right'caption='[[6tm0]]' scene=''>
<StructureSection load='6tm0' size='340' side='right'caption='[[6tm0]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TM0 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6TM0 FirstGlance]. <br>
<table><tr><td colspan='2'>[[6tm0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycpn Mycpn]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TM0 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6TM0 FirstGlance]. <br>
</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=6tm0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tm0 OCA], [http://pdbe.org/6tm0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6tm0 RCSB], [http://www.ebi.ac.uk/pdbsum/6tm0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6tm0 ProSAT]</span></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MPN_142, MP012 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272634 MYCPN])</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=6tm0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tm0 OCA], [http://pdbe.org/6tm0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6tm0 RCSB], [http://www.ebi.ac.uk/pdbsum/6tm0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6tm0 ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Mycoplasma pneumoniae is a bacterial human pathogen that causes primary atypical pneumonia. M. pneumoniae motility and infectivity are mediated by the immunodominant proteins P1 and P40/P90, which form a transmembrane adhesion complex. Here we report the structure of P1, determined by X-ray crystallography and cryo-electron microscopy, and the X-ray structure of P40/P90. Contrary to what had been suggested, the binding site for sialic acid was found in P40/P90 and not in P1. Genetic and clinical variability concentrates on the N-terminal domain surfaces of P1 and P40/P90. Polyclonal antibodies generated against the mostly conserved C-terminal domain of P1 inhibited adhesion of M. pneumoniae, and serology assays with sera from infected patients were positive when tested against this C-terminal domain. P40/P90 also showed strong reactivity against human infected sera. The architectural elements determined for P1 and P40/P90 open new possibilities in vaccine development against M. pneumoniae infections.
Immunodominant proteins P1 and P40/P90 from human pathogen Mycoplasma pneumoniae.,Vizarraga D, Kawamoto A, Matsumoto U, Illanes R, Perez-Luque R, Martin J, Mazzolini R, Bierge P, Pich OQ, Espasa M, Sanfeliu I, Esperalba J, Fernandez-Huerta M, Scheffer MP, Pinyol J, Frangakis AS, Lluch-Senar M, Mori S, Shibayama K, Kenri T, Kato T, Namba K, Fita I, Miyata M, Aparicio D Nat Commun. 2020 Oct 14;11(1):5188. doi: 10.1038/s41467-020-18777-y. PMID:33057023<ref>PMID:33057023</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6tm0" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Aparicio D]]
[[Category: Mycpn]]
[[Category: Fita I]]
[[Category: Aparicio, D]]
[[Category: Illanes R]]
[[Category: Fita, I]]
[[Category: Martin J]]
[[Category: Illanes, R]]
[[Category: Perez-Luque R]]
[[Category: Martin, J]]
[[Category: Vizarraga D]]
[[Category: Perez-Luque, R]]
[[Category: Vizarraga, D]]
[[Category: Adhesion]]
[[Category: Cell adhesion]]
[[Category: Extracellular]]
[[Category: Sugar]]

Revision as of 12:50, 18 November 2020

N-Domain P40/P90 Mycoplasma pneumoniae complexed with 6'SLN-Domain P40/P90 Mycoplasma pneumoniae complexed with 6'SL

Structural highlights

6tm0 is a 2 chain structure with sequence from Mycpn. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
NonStd Res:
Gene:MPN_142, MP012 (MYCPN)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

Mycoplasma pneumoniae is a bacterial human pathogen that causes primary atypical pneumonia. M. pneumoniae motility and infectivity are mediated by the immunodominant proteins P1 and P40/P90, which form a transmembrane adhesion complex. Here we report the structure of P1, determined by X-ray crystallography and cryo-electron microscopy, and the X-ray structure of P40/P90. Contrary to what had been suggested, the binding site for sialic acid was found in P40/P90 and not in P1. Genetic and clinical variability concentrates on the N-terminal domain surfaces of P1 and P40/P90. Polyclonal antibodies generated against the mostly conserved C-terminal domain of P1 inhibited adhesion of M. pneumoniae, and serology assays with sera from infected patients were positive when tested against this C-terminal domain. P40/P90 also showed strong reactivity against human infected sera. The architectural elements determined for P1 and P40/P90 open new possibilities in vaccine development against M. pneumoniae infections.

Immunodominant proteins P1 and P40/P90 from human pathogen Mycoplasma pneumoniae.,Vizarraga D, Kawamoto A, Matsumoto U, Illanes R, Perez-Luque R, Martin J, Mazzolini R, Bierge P, Pich OQ, Espasa M, Sanfeliu I, Esperalba J, Fernandez-Huerta M, Scheffer MP, Pinyol J, Frangakis AS, Lluch-Senar M, Mori S, Shibayama K, Kenri T, Kato T, Namba K, Fita I, Miyata M, Aparicio D Nat Commun. 2020 Oct 14;11(1):5188. doi: 10.1038/s41467-020-18777-y. PMID:33057023[1]

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

References

  1. ↑ Vizarraga D, Kawamoto A, Matsumoto U, Illanes R, Perez-Luque R, Martin J, Mazzolini R, Bierge P, Pich OQ, Espasa M, Sanfeliu I, Esperalba J, Fernandez-Huerta M, Scheffer MP, Pinyol J, Frangakis AS, Lluch-Senar M, Mori S, Shibayama K, Kenri T, Kato T, Namba K, Fita I, Miyata M, Aparicio D. Immunodominant proteins P1 and P40/P90 from human pathogen Mycoplasma pneumoniae. Nat Commun. 2020 Oct 14;11(1):5188. doi: 10.1038/s41467-020-18777-y. PMID:33057023 doi:http://dx.doi.org/10.1038/s41467-020-18777-y

6tm0, resolution 2.80Å

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