4dcb: Difference between revisions
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The | ==Y. pestis Plasminogen Activator Pla in Complex with Human Plasminogen Activation Loop Peptide ALP11== | ||
<StructureSection load='4dcb' size='340' side='right'caption='[[4dcb]], [[Resolution|resolution]] 2.03Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4dcb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Yersinia_pestis Yersinia pestis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DCB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DCB FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.033Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C8E:(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE'>C8E</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=4dcb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dcb OCA], [https://pdbe.org/4dcb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dcb RCSB], [https://www.ebi.ac.uk/pdbsum/4dcb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dcb ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/PLA_YERPE PLA_YERPE] In the mammalian host activates (cleaves) plasminogen to generate the serine protease plasmin. Plasmin degrades fibrin clots (fibrinolysis) and facilitates bacterial cell migration, enabling rapid dissemination of bacteria from the initial site of infection (Probable). Cleaves host plasminogen to generate plasmin and probably also has autocatalytic activity (PubMed:20637417, PubMed:22645135). Fibrinolytic activity prevails at 37 degrees Celsius whereas coagulase expression predominates at lower temperatures (28 degrees Celsius) (PubMed:2526282). Cleaves plasminogen; plasminogen cleavage is much higher than coagulase activity (PubMed:20637417, PubMed:22645135, PubMed:2526282, PubMed:2651310).<ref>PMID:20637417</ref> <ref>PMID:22645135</ref> <ref>PMID:2526282</ref> <ref>PMID:2651310</ref> <ref>PMID:17635705</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Omptins constitute a unique family of outer membrane proteases that are widespread in Enterobacteriaceae. The plasminogen activator (Pla) of Yersinia pestis is an omptin family member that is very important for development of both bubonic and pneumonic plague. The physiological function of Pla is to cleave (activate) human plasminogen to form the plasma protease plasmin. Uniquely, lipopolysaccharide (LPS) is essential for the catalytic activity of all omptins, including Pla. Why omptins require LPS for enzymatic activity is unknown. Here, we report the co-crystal structure of LPS-free Pla in complex with the activation loop peptide of human plasminogen, its natural substrate. The structure shows that in the absence of LPS, the peptide substrate binds deep within the active site groove and displaces the nucleophilic water molecule, providing an explanation for the dependence of omptins on LPS for enzymatic activity. | |||
Structural basis for activation of an integral membrane protease by lipopolysaccharide.,Eren E, van den Berg B J Biol Chem. 2012 Jul 6;287(28):23971-6. Epub 2012 May 29. PMID:22645135<ref>PMID:22645135</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4dcb" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Plasminogen activator|Plasminogen activator]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Yersinia pestis]] | |||
[[Category: Eren E]] | |||
[[Category: Van den Berg B]] | |||
Latest revision as of 09:53, 27 November 2024
Y. pestis Plasminogen Activator Pla in Complex with Human Plasminogen Activation Loop Peptide ALP11Y. pestis Plasminogen Activator Pla in Complex with Human Plasminogen Activation Loop Peptide ALP11
Structural highlights
FunctionPLA_YERPE In the mammalian host activates (cleaves) plasminogen to generate the serine protease plasmin. Plasmin degrades fibrin clots (fibrinolysis) and facilitates bacterial cell migration, enabling rapid dissemination of bacteria from the initial site of infection (Probable). Cleaves host plasminogen to generate plasmin and probably also has autocatalytic activity (PubMed:20637417, PubMed:22645135). Fibrinolytic activity prevails at 37 degrees Celsius whereas coagulase expression predominates at lower temperatures (28 degrees Celsius) (PubMed:2526282). Cleaves plasminogen; plasminogen cleavage is much higher than coagulase activity (PubMed:20637417, PubMed:22645135, PubMed:2526282, PubMed:2651310).[1] [2] [3] [4] [5] Publication Abstract from PubMedOmptins constitute a unique family of outer membrane proteases that are widespread in Enterobacteriaceae. The plasminogen activator (Pla) of Yersinia pestis is an omptin family member that is very important for development of both bubonic and pneumonic plague. The physiological function of Pla is to cleave (activate) human plasminogen to form the plasma protease plasmin. Uniquely, lipopolysaccharide (LPS) is essential for the catalytic activity of all omptins, including Pla. Why omptins require LPS for enzymatic activity is unknown. Here, we report the co-crystal structure of LPS-free Pla in complex with the activation loop peptide of human plasminogen, its natural substrate. The structure shows that in the absence of LPS, the peptide substrate binds deep within the active site groove and displaces the nucleophilic water molecule, providing an explanation for the dependence of omptins on LPS for enzymatic activity. Structural basis for activation of an integral membrane protease by lipopolysaccharide.,Eren E, van den Berg B J Biol Chem. 2012 Jul 6;287(28):23971-6. Epub 2012 May 29. PMID:22645135[6] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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