1rg0

From Proteopedia

(Difference between revisions)

Revision as of 07:55, 28 February 2018

Monoclinic crystal form of the truncated K122-4 pilin from Pseudomonas aeruginosa

Structural highlights

1rg0 is a 2 chain structure with sequence from "bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1qve, 1hpw, 1dzo, 1oqw, 1ayz, 1oqv
Gene:	PILA, FIMA ("Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Adherence of pathogens to host cells is critical for the initiation of infection and is thus an attractive target for anti-infective therapeutics and vaccines. In the opportunistic human pathogen Pseudomonas aeruginosa, host-cell adherence is achieved predominantly by type IV pili. Analysis of several clinical strains of P. aeruginosa reveals poor sequence conservation between pilin genes, including the residues in the receptor-binding site. Interestingly, the receptor-binding sites appear to retain a conserved surface epitope because all Pseudomonas type IV pili recognize the same receptor on the host cell and cross-reactive antibodies specific for the receptor-binding site exist. Here, we present the crystallographic analysis of two crystal forms of truncated pilin from P. aeruginosa strain K122-4 (DeltaK122-4) at 1.54 and 1.8 A resolution, respectively. The DeltaK122-4 structure is compared to other crystallographically determined type IV pilin structures and an NMR structure of DeltaK122-4 pilin. A comparison with the structure of the highly divergent P. aeruginosa strain K (DeltaPAK) pilin indicates that the receptor-binding loop in both pilins forms a shallow depression with a surface that is formed by main-chain atoms. Conservation of this putative binding site is independent of the sequence as long as the main-chain conformation is conserved and could therefore explain the shared receptor specificity and antibody cross reactivity of highly divergent Pseudomonas type IV pilins.

Crystallographic analysis of the Pseudomonas aeruginosa strain K122-4 monomeric pilin reveals a conserved receptor-binding architecture.,Audette GF, Irvin RT, Hazes B Biochemistry. 2004 Sep 14;43(36):11427-35. PMID:15350129^[1]

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

References

↑ Audette GF, Irvin RT, Hazes B. Crystallographic analysis of the Pseudomonas aeruginosa strain K122-4 monomeric pilin reveals a conserved receptor-binding architecture. Biochemistry. 2004 Sep 14;43(36):11427-35. PMID:15350129 doi:http://dx.doi.org/10.1021/bi048957s

1 Structural highlights
2 Evolutionary Conservation
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1rg0"

@@ Line 1: / Line 1: @@
 ==Monoclinic crystal form of the truncated K122-4 pilin from Pseudomonas aeruginosa==
 <StructureSection load='1rg0' size='340' side='right' caption='[[1rg0]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1qve|1qve]], [[1hpw|1hpw]], [[1dzo|1dzo]], [[1oqw|1oqw]], [[1ayz|1ayz]], [[1oqv|1oqv]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PILA, FIMA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 "Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885])</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=1rg0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rg0 OCA], [http://pdbe.org/1rg0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1rg0 RCSB], [http://www.ebi.ac.uk/pdbsum/1rg0 PDBsum]</span></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=1rg0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rg0 OCA], [http://pdbe.org/1rg0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1rg0 RCSB], [http://www.ebi.ac.uk/pdbsum/1rg0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1rg0 ProSAT]</span></td></tr>
 </table>
 == Evolutionary Conservation ==
@@ Line 11: / Line 12: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rg/1rg0_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rg/1rg0_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</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/chain_selection.php?pdb_ID=2ata 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=1rg0 ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">

1rg0

From Proteopedia

Revision as of 07:55, 28 February 2018

Monoclinic crystal form of the truncated K122-4 pilin from Pseudomonas aeruginosa

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox