Adhesin

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(New page: <StructureSection load='4f8p' size='340' side='right' caption='Adhesin PsaA complex with galactose (PDB ID 4f8p)' scene=''> '''Adhesins''' (Adh) are surface components of bacteria whi...)
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<StructureSection load='' size='350' side='right' caption='Adhesin PsaA complex with tert-butyl formate and galactose (stick model) (PDB ID [[4f8p]])' scene='70/705684/Cv/1'>
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<StructureSection load='4f8p' size='340' side='right' caption='Adhesin PsaA complex with galactose (PDB ID [[4f8p]])' scene=''>
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'''Adhesins''' (Adh) are surface components of bacteria which facillitate adhesion to surfaces or other cells. Adh are specific surface recognition protein and are regarded as virulence factors.
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== Function ==
== Function ==
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== Disease ==
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'''Adhesins''' (Adh) are surface components of bacteria which facillitate adhesion to surfaces or other cells. Adh are specific surface recognition protein and are regarded as virulence factors.<ref>PMID:11043979</ref> '''FimH''' is the ''E. coli'' adhesin which is part of the type 1 pili of the bacteria. The pili is composed of subunits '''FimF, FimG''' and '''FimD'''<ref>PMID:18369105</ref>. The main Adhesins of the pathogen ''Mycoplasma genitalium'' are '''P110''' or '''Mgp-operon protein 3''' and '''P140'''<ref>PMID:30367053</ref>. See also [[Journal:Acta Cryst D:S2059798320008116|Novel structure of the N-terminal helical domain of BibA, a Group B Streptococcus immunogenic bacterial adhesin]].
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== Relevance ==
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For trimeric autotransporter adhesin see [[EibD]].
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== Structural highlights ==
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== Disease ==
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== 3D Structures of adhesin ==
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Bacterial pathogens use adhesins as a major factor in adhesion-based virulence. Adhesins serve as vaccine targets since they are essential to infection<ref>PMID:10341176</ref>.
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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== Structural highlights ==
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{{#tree:id=OrganizedByTopic|openlevels=0|
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*Fimbrial adhesin
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<scene name='70/705684/Cv/4'>Adhesin PsaA complex with galactose, acetate and tert-butyl formate</scene> (PDB ID [[4f8p]])<ref>PMID:23277582</ref>
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*<scene name='70/705684/Cv/3'>Galactose binding site</scene>. Water molecules are shown as red spheres.
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*<scene name='70/705684/Cv/5'>Tert-butyl formate/Acetate binding site</scene>.
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**[[4k0o]], [[2bs8]] – EcF17b-G lectin domain – ''Escherichia coli'' <BR />
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== 3D Structures of adhesin ==
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**[[4b4p]], [[4bwo]] – EcFedF lectin domain <BR />
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[[Adhesin 3D structures]]
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**[[4b4q]], [[4b4r]] – EcFedF lectin domain + hexasaccharide <BR />
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**[[4w6w]], [[4w6x]], [[4w6y]] – EcFedF lectin domain + nanobody <BR />
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**[[1psz]] – SpPsaA + Zn – ''Streptococcus pneumonia''<br />
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**[[3ztt]] – SpPsaA + Mn<br />
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**[[4utp]], [[4uto]] – SpPsaA + Cd<br />
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**[[3zk7]] – SpPsaA <br />
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**[[3zk8]], [[3zk9]], [[3zka]] – SpPsaA (mutant)<br />
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**[[2bs7]] – EcF17b-G lectin domain + chitobiose <BR />
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**[[3ffo]] – EcF17b-G lectin domain + GlcNac-Man <BR />
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**[[4f8l]] – YpPsaA + galactose + inhibitor – ''Yersinia pestis'' <BR />
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**[[4f8n]] – YpPsaA + galactose + phosphate choline <BR />
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**[[4f8o]] – YpPsaA + lactose + inhibitor <BR />
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**[[4f8p]] – YpPsaA + galactose <BR />
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*Collagen adhesin (CAdh)
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</StructureSection>
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**[[1amx]] – SaCAdh CBD – ''Staphylococcus aureus''<br />
 
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**[[1d2o]] – SaCAdh B1 repeat unit<br />
 
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**[[1d2p]] – SaCAdh B1-B2 repeat units<br />
 
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**[[2f68]] – SaCAdh extracellular domain<br />
 
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**[[2f6a]] – SaCAdh extracellular domain + collagen<br />
 
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**[[2okm]] – CAdh CBD – ''Enterococcus faecalis''<br />
 
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**[[1p9h]] – YeYadA CBD – ''Yersinia enterocolitica''<br />
 
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**[[3h7x]] – YeYadA stalk domain<br />
 
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**[[3h7z]] – YeYadA stalk domain (mutant)<br />
 
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**[[3lt6]], [[3lt7]] – YeYadA coiled coil<br />
 
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**[[2lme]] – YeYadA coiled coil - NMR<br />
 
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*Adhesin
 
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**[[2odl]] – Adh secretion domain – ''Haemophilus influenzae''<br />
 
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}}
 
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</StructureSection>
 
== References ==
== References ==
<references/>
<references/>
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[[Category:Topic Page]]

Current revision

Adhesin PsaA complex with tert-butyl formate and galactose (stick model) (PDB ID 4f8p)

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References

  1. ↑ Klemm P, Schembri MA. Bacterial adhesins: function and structure. Int J Med Microbiol. 2000 Mar;290(1):27-35. PMID:11043979 doi:http://dx.doi.org/10.1016/S1438-4221(00)80102-2
  2. ↑ Nishiyama M, Ishikawa T, Rechsteiner H, Glockshuber R. Reconstitution of pilus assembly reveals a bacterial outer membrane catalyst. Science. 2008 Apr 18;320(5874):376-9. doi: 10.1126/science.1154994. Epub 2008 Mar, 27. PMID:18369105 doi:http://dx.doi.org/10.1126/science.1154994
  3. ↑ Aparicio D, Torres-Puig S, Ratera M, Querol E, Pinol J, Pich OQ, Fita I. Mycoplasma genitalium adhesin P110 binds sialic-acid human receptors. Nat Commun. 2018 Oct 26;9(1):4471. doi: 10.1038/s41467-018-06963-y. PMID:30367053 doi:http://dx.doi.org/10.1038/s41467-018-06963-y
  4. ↑ Wizemann TM, Adamou JE, Langermann S. Adhesins as targets for vaccine development. Emerg Infect Dis. 1999 May-Jun;5(3):395-403. doi: 10.3201/eid0503.990310. PMID:10341176 doi:http://dx.doi.org/10.3201/eid0503.990310
  5. ↑ Bao R, Nair MK, Tang WK, Esser L, Sadhukhan A, Holland RL, Xia D, Schifferli DM. Structural basis for the specific recognition of dual receptors by the homopolymeric pH 6 antigen (Psa) fimbriae of Yersinia pestis. Proc Natl Acad Sci U S A. 2013 Jan 15;110(3):1065-70. doi:, 10.1073/pnas.1212431110. Epub 2012 Dec 31. PMID:23277582 doi:10.1073/pnas.1212431110

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