2vqx: Difference between revisions
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< | ==Precursor of Protealysin, Metalloproteinase from Serratia proteamaculans.== | ||
<StructureSection load='2vqx' size='340' side='right'caption='[[2vqx]], [[Resolution|resolution]] 1.82Å' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2vqx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Serratia_proteamaculans Serratia proteamaculans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VQX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VQX 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]] 1.821Å</td></tr> | |||
- | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=2vqx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vqx OCA], [https://pdbe.org/2vqx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vqx RCSB], [https://www.ebi.ac.uk/pdbsum/2vqx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vqx ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q5MJ80_SERPR Q5MJ80_SERPR] Extracellular zinc metalloprotease.[RuleBase:RU366073] | |||
== 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/vq/2vqx_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2vqx ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Protealysin (PLN) belongs to the M4 family of peptidases that are commonly known as thermolysin-like proteases (TLPs). All TLPs are synthesized as precursors containing N-terminal propeptides. According to the primary structure of the N-terminal propeptides, the family is divided into two distinct groups. Representatives of the first group including thermolysin and all TLPs with known three-dimensional structures have long prosequences ( approximately 200 amino acids). Enzymes of the second group, whose prototype is protealysin, have short ( approximately 50 amino acids) propeptides. Here, we present the 1.8 A crystal structure of PLN precursor (proPLN), which is the first three-dimensional structure of a TLP precursor. Whereas the structure of the catalytic domain of proPLN is similar overall to previously reported structures of mature TLPs, it has specific features, including the absence of calcium-binding sites, and different structures of the N-terminal region and substrate-binding site. PLN propeptide forms a separate domain in the precursor and likely acts as an inhibitor that blocks the substrate-binding site and fixes the "open" conformation of the active site, which is unfavorable for catalysis. Furthermore the conserved PPL motif identified in our previous studies directly interacts with the S' subsites of the active center being a critical element of the propeptide-catalytic domain interface. Comparison of the primary structures of TLPs with short propeptides suggests that the specific features revealed in the proPLN crystal structure are typical for all protealysin-like enzymes. Thus, such proteins can be considered as a separate subfamily of TLPs. | |||
Crystal structure of the protealysin precursor: insights into propeptide function.,Demidyuk IV, Gromova TY, Polyakov KM, Melik-Adamyan WR, Kuranova IP, Kostrov SV J Biol Chem. 2010 Jan 15;285(3):2003-13. Epub 2009 Nov 13. PMID:19915005<ref>PMID:19915005</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2vqx" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Large Structures]] | ||
== | |||
< | |||
[[Category: Serratia proteamaculans]] | [[Category: Serratia proteamaculans]] | ||
[[Category: Demidyuk | [[Category: Demidyuk IV]] | ||
[[Category: Gromova | [[Category: Gromova TY]] | ||
[[Category: Kostrov | [[Category: Kostrov SV]] | ||
[[Category: Kuranova | [[Category: Kuranova IP]] | ||
[[Category: Melik-Adamyan | [[Category: Melik-Adamyan WR]] | ||
[[Category: Polyakov | [[Category: Polyakov KM]] | ||
Latest revision as of 18:29, 13 December 2023
Precursor of Protealysin, Metalloproteinase from Serratia proteamaculans.Precursor of Protealysin, Metalloproteinase from Serratia proteamaculans.
Structural highlights
FunctionQ5MJ80_SERPR Extracellular zinc metalloprotease.[RuleBase:RU366073] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedProtealysin (PLN) belongs to the M4 family of peptidases that are commonly known as thermolysin-like proteases (TLPs). All TLPs are synthesized as precursors containing N-terminal propeptides. According to the primary structure of the N-terminal propeptides, the family is divided into two distinct groups. Representatives of the first group including thermolysin and all TLPs with known three-dimensional structures have long prosequences ( approximately 200 amino acids). Enzymes of the second group, whose prototype is protealysin, have short ( approximately 50 amino acids) propeptides. Here, we present the 1.8 A crystal structure of PLN precursor (proPLN), which is the first three-dimensional structure of a TLP precursor. Whereas the structure of the catalytic domain of proPLN is similar overall to previously reported structures of mature TLPs, it has specific features, including the absence of calcium-binding sites, and different structures of the N-terminal region and substrate-binding site. PLN propeptide forms a separate domain in the precursor and likely acts as an inhibitor that blocks the substrate-binding site and fixes the "open" conformation of the active site, which is unfavorable for catalysis. Furthermore the conserved PPL motif identified in our previous studies directly interacts with the S' subsites of the active center being a critical element of the propeptide-catalytic domain interface. Comparison of the primary structures of TLPs with short propeptides suggests that the specific features revealed in the proPLN crystal structure are typical for all protealysin-like enzymes. Thus, such proteins can be considered as a separate subfamily of TLPs. Crystal structure of the protealysin precursor: insights into propeptide function.,Demidyuk IV, Gromova TY, Polyakov KM, Melik-Adamyan WR, Kuranova IP, Kostrov SV J Biol Chem. 2010 Jan 15;285(3):2003-13. Epub 2009 Nov 13. PMID:19915005[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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