2x56

<StructureSection load='2x56' size='340' side='right' caption='[[2x56]], [[Resolution|resolution]] 2.30&Aring;' scene=''>

<table><tr><td colspan='2'>[[2x56]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_pestis"_(lehmann_and_neumann_1896)_migula_1900 "bacillus pestis" (lehmann and neumann 1896) migula 1900]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X56 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2X56 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=C8E:(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE'>C8E</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2x55|2x55]], [[2x4m|2x4m]]</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Plasminogen_activator_Pla Plasminogen activator Pla], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.48 3.4.23.48] </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=2x56 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x56 OCA], [http://pdbe.org/2x56 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2x56 RCSB], [http://www.ebi.ac.uk/pdbsum/2x56 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2x56 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/COLY_YERPE COLY_YERPE]] Seems to play an essential role in plague transmission by mediating flea blockage in a temperature-dependent fashion. Fibrinolytic activity prevails at 37 degrees Celsius whereas coagulase expression predominates at lower temperatures (<30 degrees Celsius). Activates plasminogen by cleaving it.

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== Publication Abstract from PubMed ==

The plasminogen activator Pla from Yersinia pestis is an outer membrane protease (omptin) that is important for the virulence of plague. Here, we present the high-resolution crystal structure of wild-type, enzymatically active Pla at 1.9 A. The structure shows a water molecule located between active site residues D84 and H208, which likely corresponds to the nucleophilic water. A number of other water molecules are present in the active site, linking residues important for enzymatic activity. The R211 sidechain in loop L4 is close to the nucleophilic water and possibly involved in the stabilization of the oxyanion intermediate. Subtle conformational changes of H208 result from the binding of lipopolysaccharide to the outside of the barrel, explaining the unusual dependence of omptins on lipopolysaccharide for activity. The Pla structure suggests a model for the interaction with plasminogen substrate and provides a more detailed understanding of the catalytic mechanism of omptin proteases.

 

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== References ==

[[Category: Plasminogen activator Pla]]

[[Category: Berg, B van den]]

[[Category: Eren, E]]

[[Category: Goguen, J]]

[[Category: Murphy, M]]

[[Category: Aspartyl protease]]

[[Category: Transmembrane]]