1rg0: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-{{Seed}}
-[[Image:1rg0.png|left|200px]]
-<!--
+==Monoclinic crystal form of the truncated K122-4 pilin from Pseudomonas aeruginosa==
-The line below this paragraph, containing "STRUCTURE_1rg0", creates the "Structure Box" on the page.
+<StructureSection load='1rg0' size='340' side='right'caption='[[1rg0]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1rg0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RG0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RG0 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</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=1rg0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rg0 OCA], [https://pdbe.org/1rg0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rg0 RCSB], [https://www.ebi.ac.uk/pdbsum/1rg0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rg0 ProSAT]</span></td></tr>
-{{STRUCTURE_1rg0|  PDB=1rg0  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/FMP1_PSEAI FMP1_PSEAI]
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <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/initialview03.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/main_output.php?pdb_ID=1rg0 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== 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.
-===Monoclinic crystal form of the truncated K122-4 pilin from Pseudomonas aeruginosa===
+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<ref>PMID:15350129</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1rg0" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_15350129}}, adds the Publication Abstract to the page
+*[[Pilin 3D structures|Pilin 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 15350129 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_15350129}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-RG0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RG0 OCA].
-==Reference==
-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:[http://www.ncbi.nlm.nih.gov/pubmed/15350129 15350129]
 [[Category: Pseudomonas aeruginosa]]
-[[Category: Single protein]]
+[[Category: Audette GF]]
-[[Category: Audette, G F.]]
+[[Category: Hazes B]]
-[[Category: Hazes, B.]]
+[[Category: Irvin RT]]
-[[Category: Irvin, R T.]]
-[[Category: Adhesin]]
-[[Category: Lectin]]
-[[Category: Pseudomona]]
-[[Category: Type iv pilin]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 06:28:49 2008''