1q6h: Difference between revisions

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-[[Image:1q6h.png|left|200px]]
-<!--
+==Crystal structure of a truncated form of FkpA from Escherichia coli==
-The line below this paragraph, containing "STRUCTURE_1q6h", creates the "Structure Box" on the page.
+<StructureSection load='1q6h' size='340' side='right'caption='[[1q6h]], [[Resolution|resolution]] 1.97&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'>[[1q6h]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q6H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Q6H 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]] 1.97&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-{{STRUCTURE_1q6h|  PDB=1q6h  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1q6h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q6h OCA], [https://pdbe.org/1q6h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1q6h RCSB], [https://www.ebi.ac.uk/pdbsum/1q6h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1q6h ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/FKBA_ECOLI FKBA_ECOLI] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
+== 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/q6/1q6h_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=1q6h ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The protein FkpA from the periplasm of Escherichia coli exhibits both cis/trans peptidyl-prolyl isomerase (PPIase) and chaperone activities. The crystal structure of the protein has been determined in three different forms: as the full-length native molecule, as a truncated form lacking the last 21 residues, and as the same truncated form in complex with the immunosuppressant ligand, FK506. FkpA is a dimeric molecule in which the 245-residue subunit is divided into two domains. The N-terminal domain includes three helices that are interlaced with those of the other subunit to provide all inter-subunit contacts maintaining the dimeric species. The C-terminal domain, which belongs to the FK506-binding protein (FKBP) family, binds the FK506 ligand. The overall form of the dimer is V-shaped, and the different crystal structures reveal a flexibility in the relative orientation of the two C-terminal domains located at the extremities of the V. The deletion mutant FkpNL, comprising the N-terminal domain only, exists in solution as a mixture of monomeric and dimeric species, and exhibits chaperone activity. By contrast, a deletion mutant comprising the C-terminal domain only is monomeric, and although it shows PPIase activity, it is devoid of chaperone function. These results suggest that the chaperone and catalytic activities reside in the N and C-terminal domains, respectively. Accordingly, the observed mobility of the C-terminal domains of the dimeric molecule could effectively adapt these two independent folding functions of FkpA to polypeptide substrates.
-===Crystal structure of a truncated form of FkpA from Escherichia coli===
+Structural and functional studies of FkpA from Escherichia coli, a cis/trans peptidyl-prolyl isomerase with chaperone activity.,Saul FA, Arie JP, Vulliez-le Normand B, Kahn R, Betton JM, Bentley GA J Mol Biol. 2004 Jan 9;335(2):595-608. PMID:14672666<ref>PMID:14672666</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_14672666}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1q6h" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 14672666 is the PubMed ID number.
--->
-{{ABSTRACT_PUBMED_14672666}}
-==About this Structure==
-[[1q6h]] is a 2 chain structure of [[Cyclophilin]] with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q6H OCA].
 ==See Also==
-*[[Cyclophilin]]
+*[[FKBP 3D structures|FKBP 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:14672666</ref><references group="xtra"/>
+__TOC__
+</StructureSection>
 [[Category: Escherichia coli]]
-[[Category: Peptidylprolyl isomerase]]
+[[Category: Large Structures]]
-[[Category: Arie, J P.]]
+[[Category: Arie J-P]]
-[[Category: Bentley, G A.]]
+[[Category: Bentley GA]]
-[[Category: Betton, J M.]]
+[[Category: Betton J-M]]
-[[Category: Kahn, R.]]
+[[Category: Kahn R]]
-[[Category: Normand, B Vulliez-le.]]
+[[Category: Saul FA]]
-[[Category: Saul, F A.]]
+[[Category: Vulliez-le Normand B]]
-[[Category: Chaperone]]
-[[Category: Fkbp family]]
-[[Category: Heat shock protein]]
-[[Category: Peptidyl-prolyl isomerase]]
-[[Category: Periplasm]]