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== Function ==
== Function ==


'''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>.  For trimeric autotransporter adhesin see [[EibD]].
'''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]].
 
For trimeric autotransporter adhesin see [[EibD]].


== Disease ==
== Disease ==
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*<scene name='70/705684/Cv/3'>Galactose binding site</scene>. Water molecules are shown as red spheres.
*<scene name='70/705684/Cv/3'>Galactose binding site</scene>. Water molecules are shown as red spheres.
*<scene name='70/705684/Cv/5'>Tert-butyl formate/Acetate binding site</scene>.
*<scene name='70/705684/Cv/5'>Tert-butyl formate/Acetate binding site</scene>.
</StructureSection>
 
== 3D Structures of adhesin ==
== 3D Structures of adhesin ==
[[Adhesin 3D structures]]


Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
</StructureSection>
{{#tree:id=OrganizedByTopic|openlevels=0|
 
*Fimbrial adhesin
 
**[[4k0o]], [[2bs8]], [[2bsc]], [[2bsb]], [[5nwp]] – EcF17b-G lectin domain – ''Escherichia coli''  <BR />
**[[1o9z]], [[1o9w]], [[1o9v]] – EcF17a-G lectin domain  <BR />
**[[5vq5]] – EcF17 lectin domain (mutant) <BR />
**[[1oio]] – EcF17c lectin domain <BR />
**[[4b4p]], [[4bwo]] – EcF18 lectin domain  <BR />
**[[4auu]], [[1uwf]], [[1tr7]], [[5fwr]] – EcAdh  FimH lectin domain <BR />
**[[5mca]], [[5fx3]] – EcAdh  FimH lectin domain (mutant)  <BR />
**[[5afo]] – EcAdh  LF82  <BR />
**[[6aow]] – EcAdh FMLH lectin domain <BR />
**[[3zk7]] – SpPsaA - ''Streptococcus pneumoniae'' <br />
**[[3zk8]], [[3zk9]], [[3zka]] – SpPsaA (mutant)<br />
**[[3u4k]] – Adh lectin domain – ''Klebsiella pneumoniae''<BR />
 
*Fimbrial adhesion complexes
 
**[[4b4q]], [[4b4r]] – EcF18 lectin domain + hexasaccharide  <BR />
**[[4w6w]], [[4w6x]], [[4w6y]] – EcF18 lectin domain  + nanobody <BR />
**[[4j3o]] – EcAdh FimH + FimG + FimC + FimF + FimD <BR />
**[[3rfz]], [[1ze3]] – EcAdh FimH + FimC + FimD <BR />
**[[1qun]], [[1klf]], [[1kiu]] – EcAdh FimH + FimC <BR />
**[[4xo9]] – EcAdh FimH + DSG residues 24-37 <BR />
**[[4xod]], [[4xoa]] – EcAdh FimH + FimG residues 24-37 <BR />
**[[4xob]] – EcAdh FimH + FimF residues 24-37 + mannoside derivative<BR />
**[[5jr4]], [[5jqi]] – EcAdh FimH (mutant) + FimG N-terminal <BR />
**[[6as8]], [[6arm]], [[6aoy]] – EcAdh FMLD lectin domain + galactoside derivative <BR />
**[[6aox]] – EcAdh FMLD lectin domain + TF antigen <BR />
**[[6aro]] – EcAdh FMLH lectin domain + quinoline derivative <BR />
**[[5muc]], [[5l4y]], [[5l4x]], [[5l4w]], [[5l4v]], [[5l4u]], [[5l4t]], [[5jcq]], [[5jcr]], [[5f2f]], [[5f3f]], [[5abz]], [[4xo8]], [[4x5p]], [[4x5q]], [[4x5r]], [[4lov]], [[4css]], [[4cst]], [[4att]], [[4auj]], [[4auy]], [[4av0]], [[4av4]], [[4av5]], [[4avh]], [[4avi]], [[4avj]], [[4avk]], [[3zl1]], [[3zl2]], [[2vco]] – EcAdh FimH lectin domain + mannoside derivative <BR />
**[[5cgb]] – EcAdh FimH lectin domain + galactitol <BR />
**[[5ab1]], [[4x50]] – EcAdh FimH + mannoside derivative <BR />
**[[5aap]], [[5aal]], [[5mts]] – EcAdh  FimH lectin domain + anti-adhesive <BR />
**[[3f6j]], [[3f64]], [[1zpl]], [[1zk5]]  – EcF17a-G lectin domain + GlcNAc derivative <BR />
 
 
**[[1psz]] – SpPsaA + Zn – ''Streptococcus pneumonia''<br />
**[[3ztt]] – SpPsaA + Mn<br />
**[[4utp]], [[4uto]] – SpPsaA + Cd<br />
**[[2bs7]] – EcF17b-G lectin domain + chitobiose  <BR />
**[[3ffo]] – EcF17b-G lectin domain + GlcNac-Man  <BR />
**[[4b4q]], [[4b4r]] – EcFedF lectin domain + hexasaccharide  <BR />
**[[4w6w]], [[4w6x]], [[4w6y]] – EcFedF lectin domain  + nanobody <BR />
**[[4f8l]] – YpPsaA + galactose + inhibitor – ''Yersinia pestis'' <BR />
**[[4f8n]] – YpPsaA + galactose + phosphate choline <BR />
**[[4f8o]] – YpPsaA + lactose + inhibitor  <BR />
**[[4f8p]] – YpPsaA + galactose  <BR />
 
*Epitheial adhesin
 
**[[4d3w]], [[4asl]], [[4af9]] – CgAdh epithelial 1 A domain – ''Candida glabrata''<br />
**[[4afc]], [[4afb]], [[4afa]] – CgAdh epithelial 1 A domain (mutant)<br />
**[[4cp2]], [[4cp1]], [[4cp0]] – CgAdh epithelial 9 A domain <br />
**[[4coz]], [[4coy]], [[4cow]], [[4cov]], [[4cou]] – CgAdh epithelial 6 A domain <br />
 
*Collagen adhesin (CAdh)
 
**[[1amx]] – SaCAdh CBD – ''Staphylococcus aureus''<br />
**[[1d2o]] – SaCAdh B1 repeat unit<br />
**[[1d2p]] – SaCAdh B1-B2 repeat units<br />
**[[2f68]] – SaCAdh extracellular domain<br />
**[[2f6a]] – SaCAdh extracellular domain + collagen<br />
**[[2okm]], [[2z1p]] – CAdh CBD – ''Enterococcus faecalis''<br />
**[[1p9h]] – YeYadA CBD – ''Yersinia enterocolitica''<br />
**[[3h7x]] – YeYadA stalk domain<br />
**[[3h7z]] – YeYadA stalk domain (mutant)<br />
**[[3lt6]], [[3lt7]] – YeYadA coiled coil<br />
**[[2lme]] – YeYadA coiled coil - NMR<br />
 
*Serine-rich adhesin for platelets (SRAP)
 
**[[4m00]] – SaSRAP LBD<br />
**[[4m01]] – SaSRAP LBD N-terminal<br />
**[[4m02]] – SaSRAP LBD middle region<br />
**[[4m03]] – SaSRAP LBD C-terminal<br />
 
*Adhesin
 
**[[2odl]], [[2gr8]], [[2gr7]] – HiAdh secretion domain – ''Haemophilus influenzae''<br />
**[[3emf]] – HiAdh residues 51-166<br />
**[[3emi]] – HiAdh residues 307-422 (mutant)<br />
**[[1s7m]] – HiAdh residues 548-706<br />
**[[3emo]] – HiAdh residues 937-1098<br />
**[[4zh7]], [[4zh0]] – Adh BABA – ''Helicobacter pylori''<br />
**[[4usx]] – Adh trimeric autotransporter – ''Burkholderia pseudomallei''<br />
**[[3wqa]], [[3wpr]], [[3wpp]], [[3wpo]], [[3wpa]] – AcAdh trimeric autotransporter C-terminal – ''Acinetobacter''<br />
**[[3wp8]] – AcAdh trimeric autotransporter C-terminal (mutant)<br />
**[[4err]] – Adh autotransporter effector domain – ''Vibrio vulnificus''<br />
**[[2wps]], [[2wpr]], [[2wpq]] – Adh trimeric autotransporter residues 483-523 – ''Salmonella enterica''<br />
**[[4tsh]] – Adh surface protein – ''Streptococcus mutans''<br />
**[[4mee]] – EcAdh diffuse adherence C-terminal <br />
**[[5lvy]] – EcAdh lectin domain  <BR />
**[[3etw]] – FnAdh  A – ''Fusobacterium nucleatum'' <BR />
**[[3etz]], [[3ety]], [[3etx]], [[2gl2]] – FnAdh  A (mutant)  <BR />
**[[3d9x]] – Adh  A – ''Bartonella henselae'' <BR />
**[[2lwb]] – Adh  WI-1 – ''Ajellomyces dermatitidis'' <BR />
**[[5my7]] – Adh  – ''Neisseria meningitidis'' <BR />
}}




Latest revision as of 13:38, 22 July 2021


Function

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.[1] 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[2]. The main Adhesins of the pathogen Mycoplasma genitalium are P110 or Mgp-operon protein 3 and P140[3]. See also Novel structure of the N-terminal helical domain of BibA, a Group B Streptococcus immunogenic bacterial adhesin.

For trimeric autotransporter adhesin see EibD.

Disease

Bacterial pathogens use adhesins as a major factor in adhesion-based virulence. Adhesins serve as vaccine targets since they are essential to infection[4].

Structural highlights

(PDB ID 4f8p)[5]

  • . Water molecules are shown as red spheres.
  • .

3D Structures of adhesin

Adhesin 3D structures


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

Drag the structure with the mouse to rotate


ReferencesReferences

  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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