2xrm: Difference between revisions

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-[[Image:2xrm.jpg|left|200px]]
-<!--
+==Processed Intracellular subtilisin from B. clausii==
-The line below this paragraph, containing "STRUCTURE_2xrm", creates the "Structure Box" on the page.
+<StructureSection load='2xrm' size='340' side='right'caption='[[2xrm]], [[Resolution|resolution]] 2.60&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'>[[2xrm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Alkalihalobacillus_clausii Alkalihalobacillus clausii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XRM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XRM 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]] 2.6&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SR:STRONTIUM+ION'>SR</scene></td></tr>
-{{STRUCTURE_2xrm|  PDB=2xrm  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2xrm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xrm OCA], [https://pdbe.org/2xrm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xrm RCSB], [https://www.ebi.ac.uk/pdbsum/2xrm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xrm ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/D0AB41_ALKCL D0AB41_ALKCL]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+A distinct class of the biologically important subtilisin family of serine proteases functions exclusively within the cell and forms a major component of the bacilli degradome. However, the mode and mechanism of posttranslational regulation of intracellular protease activity are unknown. Here we describe the role played by a short N-terminal extension prosequence novel amongst the subtilisins that regulates intracellular subtilisin protease (ISP) activity through two distinct modes: active site blocking and catalytic triad rearrangement. The full-length proenzyme (proISP) is inactive until specific proteolytic processing removes the first 18 amino acids that comprise the N-terminal extension, with processing appearing to be performed by ISP itself. A synthetic peptide corresponding to the N-terminal extension behaves as a mixed noncompetitive inhibitor of active ISP with a K(i) of 1 muM. The structure of the processed form has been determined at 2.6 A resolution and compared with that of the full-length protein, in which the N-terminal extension binds back over the active site. Unique to ISP, a conserved proline introduces a backbone kink that shifts the scissile bond beyond reach of the catalytic serine and in addition the catalytic triad is disrupted. In the processed form, access to the active site is unblocked by removal of the N-terminal extension and the catalytic triad rearranges to a functional conformation. These studies provide a new molecular insight concerning the mechanisms by which subtilisins and protease activity as a whole, especially within the confines of a cell, can be regulated.
-===PROCESSED INTRACELLULAR SUBTILISIN FROM B. CLAUSII===
+Regulation of an intracellular subtilisin protease activity by a short propeptide sequence through an original combined dual mechanism.,Gamble M, Kunze G, Dodson EJ, Wilson KS, Jones DD Proc Natl Acad Sci U S A. 2011 Mar 1;108(9):3536-41. Epub 2011 Feb 9. PMID:21307308<ref>PMID:21307308</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2xrm" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_21307308}}, adds the Publication Abstract to the page
+*[[Subtilisin 3D structures|Subtilisin 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 21307308 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_21307308}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Alkalihalobacillus clausii]]
-[[2xrm]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_clausii Bacillus clausii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XRM OCA].
+[[Category: Large Structures]]
+[[Category: Dodson EJ]]
-==Reference==
+[[Category: Gamble M]]
-<ref group="xtra">PMID:21307308</ref><references group="xtra"/>
+[[Category: Jones DD]]
-[[Category: Bacillus clausii]]
+[[Category: Kunze G]]
-[[Category: Subtilisin]]
+[[Category: Wilson KS]]
-[[Category: Dodson, E J.]]
-[[Category: Gamble, M.]]
-[[Category: Jones, D D.]]
-[[Category: Kunze, G.]]
-[[Category: Wilson, K S.]]