3t1u: Difference between revisions
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[[ | ==Crystal Structure of the complex of Cyclophilin-A enzyme from Azotobacter vinelandii with sucAFPFpNA peptide== | ||
<StructureSection load='3t1u' size='340' side='right' caption='[[3t1u]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3t1u]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii_dj Azotobacter vinelandii dj]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T1U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3T1U FirstGlance]. <br> | |||
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NIT:4-NITROANILINE'>NIT</scene>, <scene name='pdbligand=SIN:SUCCINIC+ACID'>SIN</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3t17|3t17]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Avin_23510 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=322710 Azotobacter vinelandii DJ])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </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=3t1u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t1u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3t1u RCSB], [http://www.ebi.ac.uk/pdbsum/3t1u PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Cyclophilins constitute a class of peptidyl-prolyl isomerases which participate in processes related to protein folding, signalling and chaperoning. The crystal structure of the cytoplasmic cyclophilin A (CyPA) from the bacterium Azotobacter vinelandii complexed with a synthetic tetrapeptide was determined by molecular replacement at 2 resolution. The proline in the tetrapeptide is observed to adopt the cis-isomer conformation. Comparisons of this structure with other CyPA structures provide insights into the conformational variability, effects of peptide binding and structure-function relationships of this enzyme. | |||
Structure of a bacterial cytoplasmic cyclophilin A in complex with a tetrapeptide.,Christoforides E, Dimou M, Katinakis P, Bethanis K, Karpusas M Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Mar 1;68(Pt 3):259-64., Epub 2012 Feb 15. PMID:22442217<ref>PMID:22442217</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
== | __TOC__ | ||
</StructureSection> | |||
[[Category: Azotobacter vinelandii dj]] | [[Category: Azotobacter vinelandii dj]] | ||
[[Category: Peptidylprolyl isomerase]] | [[Category: Peptidylprolyl isomerase]] | ||
[[Category: Bethanis, K | [[Category: Bethanis, K]] | ||
[[Category: Christoforides, E | [[Category: Christoforides, E]] | ||
[[Category: Dimou, M | [[Category: Dimou, M]] | ||
[[Category: Karpusas, M | [[Category: Karpusas, M]] | ||
[[Category: Katinakis, P | [[Category: Katinakis, P]] | ||
[[Category: Isomerase]] | [[Category: Isomerase]] | ||
[[Category: Peptidyl-prolyl isomerase]] | [[Category: Peptidyl-prolyl isomerase]] | ||
[[Category: Ppiase]] | [[Category: Ppiase]] | ||